Crystallised catalytic domain of matrix metalloproteinase 9 (mmp9) and the use of its three dimensional structure to design mmp9 modulators

ABSTRACT

The invention provides a crystalline form of a polypeptide corresponding to the catalytic domain of a matrix metalloproteinase protein, MMP9. The active site binding region of the MMP9 protein is defined by its amino acid residues and their atomic coordinates. This three dimensional structure may be used to select or design chemical modulators or MMP9, particularly MMP9 inhibitors. These modulators may be used to treat a metalloproteinase mediated disease or condition.

FIELD OF THE INVENTION

[0001] This invention relates to the crystallised catalytic domain of matrix metalloproteinase 9 (MMP9) and the use of its three dimensional structure to design MMP9 modulators.

BACKGROUND OF THE INVENTION

[0002] Active proteins, such as enzymes, involved in physiological and pathological processes are important targets in the development of pharmaceutical compounds and treatments. Knowledge of the three dimensional (tertiary) structure of active proteins allows the rational design of mimics or modulators of such proteins. By searching structural databases of compounds using structural parameters derived from the active protein of interest, it is possible to select compound structures that may mimic or interact with these parameters. It is then possible to synthesise the selected compound and test its activity. Alternatively, the structural parameters derived from the active protein of interest may be used to design and synthesise a mimic or modulator with the desired activity. Such mimics or modulators may be useful as therapeutic agents for treating certain diseases. For example, WO98/07835 discloses crystal structures of a protein tyrosine kinase optionally complexed with one or more compounds. The atomic coordinates of the enzyme structures and any of the bound compounds are used to determine the three dimensional structures of kinases with unknown structure and to identify modulators of kinase functions. As another example, WO99/01476 discloses the crystal structures of anti-Factor IX Fab fragments (antibodies) and their use to identify and design new anticoagulant agents.

[0003] Knowledge of the three dimensional structure of an active protein is essential for the rational design of mimics or modulators of that protein. Lack of structural knowledge is a barrier to the development of new mimics or modulators that may have extremely useful pharmaceutical properties. The present invention relates to the previously unknown three dimensional structure of matrix metalloproteinase 9 (MMP9) and its use.

[0004] The matrix metalloproteinase (MMPs) are a family of structurally-related zinc-containing endopeptidases which mediate the breakdown of connective tissue macro-molecules. The mammalian MMP family is composed of at least twenty enzymes, classically divided into four sub-groups based on substrate specificity and domain structure (Alexander & Werb, 1991; Murphy & Reynolds, 1993; Birkedal-Hansen, 1995). The sub-groups are the collagenases (such as MMP1, MMP8, MMP13), the stromelysins (such as MMP3, MMP10, MMP11), the gelatinases (such as MMP2, MMP9) and the membrane-type MMPs (such as MMP14, MMP15, MMP16, MMP17). Enzyme activity is normally regulated in vivo by tissue inhibitors of metalloproteinases (TIMPs).

[0005] Because of their central role in re-modelling connective tissue, both as part of normal physiological growth and repair and as part of disease processes, there has been substantial interest in these proteins as targets for therapeutic intervention in a wide range of degenerative and inflammatory diseases, such as arthritis, atherosclerosis, and cancer (Whittaker et al, 1999). It was in the context of cell movement in malignancy that the gelatinases MMP2 and MMP9 were described, through their ability to degrade basement membranes as well as other matrix components (Liotta et al 1981; Collier et al 1988; Wilhelm et al 1989).

[0006] MMP9 (92 kDa Gelatinase) is a secreted protein which was first purified, then cloned and sequenced by Wilhelm et al (1989). The review of MMP9 by Vu & Werb (1998) provides an excellent source for detailed information and references on this protease. The expression of MMP9 is restricted normally to a few cell types, including trophoblasts, osteoclasts, neutrophils and macrophages. However, its expression can be induced in these same cells and in other cell types by several mediators, including exposure of the cells to growth factors or cytokines. These are the same mediators often implicated in initiating an inflammatory response. As with other secreted MMPs, MMP9 is released as an inactive Pro-enzyme or precursor which includes a propeptide domain. The Pro-enzyme is subsequently cleaved to form the active enzyme. The balance of active MMP9 versus inactive enzyme is further regulated in vivo by interaction with TIMP-1 (Tissue Inhibitor of Metalloproteinases-1), a naturally-occurring protein. TIMP-1 binds to the C-terminal region of MMP9, leading to inhibition of the catalytic domain of MMP9. The balance of induced expression of ProMMP9, cleavage of Pro- to active MMP9 and the presence of TIMP-1 combine to determine the amount of catalytically active MMP9 which is present at a local site. Proteolytically active MMP9 attacks substrates which include gelatin, elastin, and native Type IV and Type V collagens. It has no activity against native Type I collagen, proteoglycans or laminins.

[0007] Enzymes of the MMP9 and MMP2 subfamilies are similar in many ways. For example, their most distinctive catalytic property is a near absolute requirement for leucine at the substrate P1 position (protein S1 position). However, despite these similarities, MMP9 and MMP2 show a different substrate specificity. Thus MMP9 and MMP2 are clearly different enzymes although they are homologs (similar proteins having a certain degree of sequence identity but with distinct and different activity profiles).

[0008] Human MMPs are generally composed of three domains: the N-terminal propeptide domain, the protease or catalytic domain (the zinc-binding domain), and the C-terminal hemopexin-like domain. The gelatinases MMP2 and MMP9 also contain an additional domain composed of three fibronectin repeats inserted in tandem within the catalytic domain. The active site binding region lies within the catalytic domain and incorporates the S1′ pocket (also called the S1′ specificity pocket or the S1′ selectivity pocket) and the S1 pocket. It is known that the catalytic domain of certain MMPs is folded into a compact domain approximately 40×40×30 Å in size, consisting of a five-stranded β-sheet and three α-helices (Lovejoy et al. 1999; Morgunova et al. 1999; Dhanaraj et al. 1999; Moy et al. 2000; Zhang et al. 2000; Chen et al. 2000; Dhanaraj et al. 1996; Becker et al. 1995; Gooley et al. 1994; Van Doren et al. 1995; Borkakoti et al. 1994; Lovejoy et al. 1994; Lovejoy et al. 1994a; Spurlino et al. 1994; Browner et al. 1995; Moy et al. 1997; Moy et al. 1998; Moy et al. 1999; Stams et al. 1994; Finzel et al. 1998; Stockman et al. 1998; Pavlovsky et al. 1999; Gomis-Rüth et al. 1997 Li et al. 1995; Reinemer et al. 1994; Bode et al. 1994; Grams et al. 1995; Grams et al. 1995a; Esser et al. 1997). However the three dimensional structure of MMP9 has not previously been disclosed.

[0009] The largest structural differences within the catalytic domains of various MMPs are the conformation of surface loops. The S1′ specificity pocket has been described for certain MMPs, including MMP2 (Dhanaraj et al. 1999), MMP13 (Lovejoy et al. 1999), stromelysin (Dhanaraj et al. 1996), fibroblast collagenase and matrilysin (Lovejoy et al. 1999; Lovejoy et al. 1994; Lovejoy et al. 1994a; Browner et al. 1995). Among members of the MMP family, the S1′ loops do not share amino acid sequence similarity and also differ in length. The S1′ loop has no regular secondary structure in any MMP for which a structure has been determined. Thus, both the structural variability and the sequence variability of the S1′ loops contribute to the variation in overall size and shape of the S1′ pockets in the different MMPs.

[0010] There is a growing body of data implicating roles for MMP9 in various physiological and pathological processes. Physiological roles include the invasion of embryonic trophoblasts through the uterine epithelium in the early stages of embryonic implantation, some role in the growth and development of bones, and migration of inflammatory cells from the vasculature into tissues. Increased MMP9 expression has been observed in certain pathological conditions, thereby implicating MMP9 in disease processes such as asthma, arthritis, tumour metastasis, Alzheimer's, Multiple Sclerosis, and atherosclerosis.

[0011] Whilst the importance of the MMP family in the pathogenesis of arthritis and cancer has been well documented over many years, it is only relatively recently that MMPs and their inhibitors have been shown also to be important in connective tissue re-modelling in diseases of the cardiovascular system, such as atherosclerosis (Henney et al, 1991; Galis et al, 1994; Dollery et al, 1995). Various members of the MMP family have been shown to be expressed in atherosclerotic lesions of various types, but MMP9 is consistently seen in inflammatory atherosclerotic lesions, typically expressed by lipid laden macrophages. Evidence from histological investigations and molecular genetic studies implicates MMP9 over-expression in the vascular re-modelling events preceding plaque rupture, the most common cause of acute myocardial infarction (Brown et al, 1995). More recently, animal studies have shown that reducing MMP9 activity, either by genetic manipulation or through pharmacological intervention, has an impact on ventricular re-modelling following infarction and as such may represent a key mechanism in the pathogenesis of heart failure (Rhode et al 1999).

[0012] A number of MMP inhibitor compounds are known and some are being developed for pharmaceutical uses (see for example the review by Beckett & Whittaker, 1998). Different classes of compounds may have different degrees of potency and selectivity for inhibiting various MMPs. Whittaker M. et al (1999) review a wide range of known MMP inhibitor compounds. They state that an effective MMP inhibitor requires a zinc binding group or ZBG (functional group capable of chelating the active site zinc(II) ion), at least one functional group which provides a hydrogen bond interaction with the enzyme backbone, and one or more side chains which undergo effective van der Waals interactions with the enzyme subsites. Zinc binding groups in known MMP inhibitors include hydroxamates, reverse hydroxamates, thiols, carboxylates and phosphonic acids.

[0013] The structures of several hydroxamate-MMP complexes have been determined (Dhanaraj et al. 1996; Lovejoy et al. 1999; Li et al., 1995; Spurlino et al. 1994; Reinemer et al. 1994; Bode et al. 1994; Grams et al. 1995; Grams et al. 1995a; Browner et al. 1995; Stams et al., 1994; Van Doren et al. 1995; Borkakoti et al. 1994), including an MMP2-hydroxamate complex (Dhanaraj et al. 1999) and two recent solution structures of the catalytic fragment of human collagenase-3 (MMP13) complexed with a non-peptidic sulphonamide hydroxamic acid inhibitor (Moy et al. 2000; Zhang et al. 2000). However there has been no structural analysis of an MMP bound to a reverse hydroxamate. Reverse hydroxamate inhibitors may have better pharmaco-kinetic properties than their hydroxamate counterparts and therefore may present a more useful starting point for drug design.

[0014] There has been some investigation of MMP mutants showing that specific mutations do not affect the shape of the active site (Steele et al. 2000). For example, Morgunova et al (1999) designed an MMP2 mutant (Glu404Ala) to prevent autoproteolyis, preserving the intact propeptide (pro-MMP2), and the mutation had no influence on the architecture of the active site.

[0015] Chen et al. 2000 used the high-resolution NMR solution structure of the catalytic fragment of MMP13 (human collagenase-3) as a starting point for structure-based design of selective inhibitors for MMP13. Skiles et al (2001) reviewed the design, structure and therapeutic application of MMP inhibitors. They also discussed the structural characteristics of certain MMP enzymes and the binding of inhibitors to these enzymes. However the three dimensional structure of MMP9 is not known and is difficult to elucidate. No-one has been able to obtain crystals of any part of MMP9 of sufficient quality for determining the three dimensional structure of the catalytic domain and active site of MMP9.

[0016] We have now overcome the difficulties to produce crystals of the MMP9 catalytic domain that are of sufficient quality to determine the three dimensional structure of the protein by X-ray diffraction methods. There is a clear need for this MMP9 structural information to enable identification and structure-based design of new MMP9 modulators (preferably inhibitors) for the treatment of various diseases or conditions.

BRIEF DESCRIPTION OF THE DRAWINGS

[0017]FIG. 1 is a schematic representation of the three dimensional structure of the wild type MMP9:reverse hydroxamate complex.

[0018]FIG. 2 is a stereo diagram of the wild type MMP9:reverse hydroxamate complex.

[0019]FIG. 3 is a diagram showing a close-up of the MMP9 mutant (E402Q):reverse hydroxamate complex together with a portion of the (2Fo-Fc) electron density map.

[0020]FIG. 4 is a diagram showing superposition of the MMP9 mutant (E402Q) and wild type MMP9 active sites.

[0021]FIG. 5 is a Grasp representation of the MMP9 active site binding region with bound ligand.

[0022]FIG. 6 is a schematic represetation of the three dimensional structure of MMP2 oriented to maximize alignment with the structure of the MMP9:reverse hydroxamate complex shown in FIG. 1.

[0023]FIG. 7 shows the aligned amino acid sequences of MMP9 (SEQ ID NO 2) and MMP2 (SEQ ID NO 1).

DESCRIPTION OF THE INVENTION

[0024] According to a first aspect of the invention, we provide an MMP9 crystal. In particular we provide a crystalline form of a polypeptide corresponding to the catalytic domain of an MMP9 protein. The catalytic domain may be found within the complete MMP9 protein or within a fragment of the MMP9 protein. The catalytic domain may be derived from a wild type MMP9 protein or from an MMP9 mutant or variant. A mutant is a wild type MMP9 protein having one or more changes in its amino acid sequence. An MMP9 mutant may have the same activity as the wild type protein, may have a modified activity or may be inactive. A variant is a wild type or mutant MMP9 protein having one or more portions of its amino acid sequence removed, so that the variant is a different length to the wild type or mutant protein. A variant usually has the same activity as the original wild type or mutant MMP9.

[0025] The invention provides crystals of sufficient quality to determine the three dimensional structure to high resolution of any portion of the MMP9 catalytic domain.

[0026] According to a further aspect of the invention, we provide a crystalline form of a polypeptide corresponding to the catalytic domain of an MMP9 protein in complex with an MMP9 inhibitor compound. For example, the MMP9 inhibitor compound may have a reverse hydroxamate zinc binding group. Such reverse hydroxamates include, for example, compounds of Formula I:

[0027] Using X-ray crystallography we have determined the three dimensional molecular structure of an MMP9 catalytic domain. We have also determined the unique shape of an MMP9 active site binding region (defined by the atomic coordinates of its amino acids). Further, we have determined the spatial arrangement of an MMP9 inhibitor relative to the MMP9 active site binding region. The structural information can be stored on a computer-readable medium and may be used for rational drug design.

[0028] One of the major hurdles in the crystallisation of multidomain proteins is their flexibility. To increase the chances of crystallising MMP9, we used a variant construct (an enzyme construct limited to the catalytic domain with the fibronectin domain excised). This provided a rigid and compact domain.

[0029] Another major hurdle in the crystallisation and structure determination of MMP9 is that the MMP9 catalytic domain is aggressively autolytic. We therefore purified wild-type MMP9 in the presence of an inhibitor and then crystallised the purified complex. Addition of an inhibitor during the refolding step following urea denaturation is essential for prevention of N-terminal degradation and the formation of well-ordered crystals.

[0030] Weak inhibitors such as acetohydroxamic acid prevent autodegradation of the wild type MMP9 protein during refolding. However we found that weak inhibitors are not sufficiently potent to prevent autodegradation of the wild type MMP9 protein during storage or during the period of crystallisation, rendering crystallographic studies on such complexes extremely difficult. In order to form crystals of complexes with wild type protein, it is necessary to replace the weak inhibitor with a much more potent inhibitor (such as a compound of Formula I) during the final purification step before crystallisation. This limits the usefulness of the wild type construct for rational drug design using less potent inhibitors.

[0031] To overcome the problems and limitations, we designed an inactive mutant of the MMP9 catalytic domain in which the essential active site glutamate (amino acid residue E) was mutated to glutamine (amino acid residue Q). The MMP9 mutant is known as E402Q and is inactive. Use of the more stable mutant for crystallisation prevents autodegradation. It also enables stable MMP9 complexes to be crystallised with weak inhibitors by co-crystallisation. It should also be possible to crystallise the mutant protein without the inhibitor, followed by soaking of the crystals with weak or strong inhibitors.

[0032] We determined the three dimensional structure of the catalytic domain of wild type MMP9 in complex with a peptidic reverse hydroxamate inhibitor (compound of Formula I) by X-ray diffraction analysis at a nominal resolution of 2.3 Å. We also determined the three dimensional structure of the catalytic domain of the inactive MMP9 mutant (E402Q) in complex with the same inhibitor at a nominal resolution of 2.1 Å. The E to Q mutation does not change the three dimensional structure of the MMP9 enzyme.

[0033]FIG. 1 is a schematic representation of the three dimensional structure of the wild type MMP9:reverse hydroxamate complex. The S1′ specificity pocket and the region from where the three fibronectin repeats were deleted are indicated. The inhibitor is shown in all-atom representation, zinc and calcium ions are represented by dark grey and light grey spheres respectively. FIG. 1 was generated using the programs BOBSCRIPT (Esnouf 1997) and RASTER3D (Bacon & Anderson 1998; Merritt & Murphy 1994).

[0034]FIG. 2 is a stereo diagram of the wild type MMP9:reverse hydroxamate complex. It shows some of the interactions between the bound peptidic reversed hydroxamate inhibitor (compound of Formula I) and MMP9. A short hydrogen bond (2.5 Å) is formed between Glu402 and the inhibitor.

[0035]FIG. 3 is a diagram showing a close-up of the MMP9 mutant (E402Q):reverse hydroxamate complex together with a portion of the (2Fo-Fc) electron density map.

[0036]FIG. 4 is a diagram showing superposition of the MMP9 mutant (E402Q) and wild type active sites. The mutant structure is coloured light grey; the wild type structure is coloured dark grey. The structure is perturbed little on introduction of the mutant. The short hydrogen bond to the inhibitor seen in the wild type complex is absent in the mutated structure (the corresponding atoms are 3.5 Å apart in one of the molecules in the crystal asymmetric unit; in the second molecule, Oε of Gln402 is only 3.2 Å away from O1 of the inhibitor). FIG. 4 was generated using BOBSCRIPT (Esnouf 1997).

[0037]FIG. 5 is a Grasp representation of the MMP9 active site binding region with bound ligand (reverse hydroxamate compound of Formula I). FIG. 5 was generated using the program GRASP (Nicholls 1991).

[0038] The catalytic domain of MMP9 (minus the fibronectin repeats) is folded into a compact domain approximately 40×40×30 Å in size, consisting of a five-stranded β-sheet and three α-helices as found for other MMPs.

[0039] From the three dimensional structure determined for MMP9, we have found that the active site binding region in MMP9 is uniquely defined by the atomic co-ordinates of its constituent amino acid residues. These amino acid residues are listed in Table 1. TABLE 1 Phe110, Glu111, Tyr179, Pro180, Asp185, Gly186, Leu187, Leu188, Ala189, His190, Ala191, Phe192, Pro193, Lys214, Gly215, Gln391, Gly392, Tyr393, Leu397, Val398, His401, Glu402, His405, Gly408, Leu409, Asp410, His411, Pro415, Glu416, Ala417, Leu418, Tyr420, Pro421, Met422, Tyr423, Arg424, Phe425, Thr426, Glu427, Gly428, Pro429, Pro430, Leu431, His432, and Lys433.

[0040] In MMP9 the catalytic centre is composed of the active-site zinc and the essential glutamate. The residues which chelate the catalytic zinc are His401, His405, and His411. The catalytic glutamate is Glu4O2. The numbering refers to the sequential numbering of the full-length human pro-MMP9 as defined in the Swissprot protein sequence database under accession number P14780.

[0041] The atomic coordinates for wild type and the MMP9 mutant (E402Q) are shown in Tables 2 and 3 at the end of this docunent. The Tables also give the atomic coordinates of the inhibitor compound in complex with the enzyme.

[0042] The term “atomic co-ordinates” refers to mathematical co-ordinates corresponding to the positions of every atom derived from mathematical equations related to the diffraction patterns obtained from a monochromatic beam of X-rays illuminating a crystal. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are used to establish the positions of the individual atoms within the unit cell of the crystal. The term “unit cell” refers to the basic building block from which the entire volume of a crystal may be constructed. Those of skill in the art understand that a set of atomic co-ordinates determined by X-ray crystallography is not without experimental variation.

[0043] Table 2 lists the atomic coordinates in Protein Data Bank (PDB) format of the wild type MMP9 construct in complex with the reverse hydroxamate compound of Formula I. Table 3 lists the atomic coordinates in Protein Data Bank (PDB) format of the MMP9 mutant (E402Q) in complex with the reverse hydroxamate compound of Formula I. In both Tables the atomic coordinates are listed in those lines that begin with the code ATOM or HETATM, one atom per line. Following the code are: the unique atom number; the atom name; the amino acid residue name; the protein chain identifier; the amino acid residue number; the atomic coordinates x, y, and z in orthogonal Angstrom space; the atomic occupancy factor; the atomic temperature factor; the chain identifier; and the atom type. The atomic coordinates of the inhibitor compound carry the residue name of FRA. Solvent water molecules carry the residue name of HOH.

[0044] It is possible to reproduce the shape of the MMP9 active site binding region through carrying out similar structure determinations with minor changes in the experimental conditions (including changes in crystallisation conditions, crystal form, construct, etc). It will be appreciated that the atomic coordinates of the MMP9 active site binding region may vary within certain limits due to experimental variation. Such variation includes standard error (coordinates determined for the same construct may vary somewhat, for example Within 0.3 Å) and other variation (for example, coordinates of MMP9 mutants or variants). Therefore the shape of the active site binding region is defined by the set of all possible structures that contain C-alpha (Ca) atomic coordinates within 1.5 Å of the C-alpha positions of the MMP9 active site binding region residues defined above, when the two protein structures are superposed (placed on a common frame). The criterion of 1.5 Å is selected as appropriate because it is large enough to allow for experimental variation whereas it is small enough to discriminate between MMP9 and the most similar homolog MMP2.

[0045] According to a further aspect of the invention, we provide a crystalline form of a polypeptide corresponding to the active site binding region of an MMP9 protein wherein the active site binding region amino acid residues are identical or equivalent to those listed in Table 1 and the shape of the active site binding region is defined by the atomic coordinates given in Table 2 or Table 3 or by equivalent coordinates.

[0046] An amino acid residue is equivalent to a residue listed in Table I if it occurs within an MMP9 protein (including mutants and variants) at a position listed in Table 1.

[0047] Equivalent coordinates are those containing C-alpha (Cα) atomic coordinates within 1.5 Å of the C-alpha coordinates of the MMP9 active site binding region residues defined in Tables 2 or 3, when the polypeptide structures are superposed. Those skilled in the art will recognise the C-alpha positions in the active site binding region of the MMP9 protein particular positions of the amino acid side chains on the main protein chain). If the atomic coordinates of any particular C-alpha varies more than 1.5 Å from that defined in Tables 2 or 3, the protein structure does not have equivalent coordinates.

[0048] The invention provides the first structure determination of an MMP bound to a reverse hydroxamate (compound of Formula 1). The reverse hydroxamate inhibitor forms a short complementary strand similar to the known peptidic hydroxamate inhibitor complexes of other MMPs and binds the catalytic zinc in a similar manner to both the peptidic and non-peptidic hydroxamate inhibitor complexes of other MMPs. The structure we have determined includes the three dimensional coordinates of the reverse hydroxamate inhibitor giving previously unknown information about its spatial orientation in the MMP9 active site and details of interactions between the reverse hydroxamate inhibitor and MMP9.

[0049] In the wild type MMP9-reverse hydroxamate inhibitor complex, the inhibitor spans the S1 and S1′ pockets. Four hydrogen bonds are formed between the inhibitor and the protein main chain (interactions with the backbone amides of Leu189, Tyr423, and the carbonyl oxygen atoms of Pro421, Gly187). The side-chain of P1 leucine of the peptidic inhibitor is located in a large S1 pocket; the tertiary butyl group points out to solvent. The co-ordination of the catalytic zinc by His401, His405 and His411 is completed by both hydroxamate oxygen atoms of the inhibitor, in a distorted penta-coordinate geometry. One of the zinc-chelating oxygen atoms (O1) forms a short (2.5 Å) hydrogen bond with Glu402. Oxygen O1 also interacts with His405 and has a water-mediated interaction with the backbone amide of Ala192 (water molecule only visible in the electron density for one of the protein molecules in the crystal asymmetric unit). The other chelating oxygen (O2) interacts with His411 and with the carbonyl of Pro421 via a water molecule (water molecule only visible in the electron density for one of the protein molecules in the crystal asymmetric unit).

[0050] The structure of the MMP9 mutant catalytic domain shows no significant deviation from the wild type structure. The same reverse hydroxamate inhibitor was used in the wild-type and mutant complexes to show that the active site shape is not changed on introduction of the mutation. The only minor difference in structure is that the distance between Glu402 and the hydroxamate moiety in the mutant complex is too long to be considered hydrogen-bonding distance. Apart from this small discrepancy, the wild type and mutant MMP9 structures are identical.

[0051] The MMP9 protein is similar to the MMP2 protein in tertiary and quaternary structure as well as in some features associated with its catalytic activity. In addition these two proteins interact with inhibitors in very similar ways in the S1 pocket. However the active site binding region (S1′ pocket) of MMP9 is strikingly different from that of MMP2 in size and chemical composition. This difference provides a structural basis for understanding the difference in specificity between the two enzyme types.

[0052]FIG. 6 is a schematic representation showing the three dimensional structure of MMP2 oriented to maximize alignment with the structure of the MMP9:reverse hydroxamate complex shown in FIG. 1. FIG. 6 shows superposition of the MMP9 and MMP2 catalytic domain structures (using deposited co-ordinates 1QIB, Dhanaraj et al. 1999). MMP9 is coloured light grey; MMP2 is coloured dark grey. The MMP9 inhibitor is shown in all-atom representation. The two zinc ions per catalytic domain are represented by light (MMP9) and dark (MMP2) spheres. The two structures are similar with the only significant differences being in the S1′ specificity pocket and in the region of the fibronectin deletions. Differences observed at the N-terminus are unlikely to be significant as the N-terminus of MMP9 is closer to the intact pro-MMP2 structure in this region (Morgunova et al. 1999).

[0053]FIG. 7 shows the amino acid sequences of MMP9 (SEQ ID NO 2) and MMP2 (SEQ ID NO 1), aligned by PILEUP—capital letters indicate identity of amino acid residue between MMP2 and MMP9. Amino acids are abbreviated by one letter codes: A = ALA = alanine C = CYS = cysteine D = ASP = aspartate E = GLU = F = PHE = phenylalanine G = GLY = glycine glutamate H = HIS = histidine I = ILE = isoleucine K = LYS = lysine L = LEU = leucine M = MET = methionine N = ASN = asparagine P = PRO = proline Q = GLN = glutamine R = ARG = arginine S = SER = serine T = THR = threonine V = VAL = valine W = TRP = Y = TYR = tyrosine. tryptophan

[0054] Both the MMP9 and the MMP2 are full-length human sequences: each is the sequence of the Pro-enzyme including the propeptide domain. The MMP9 sequence is derived from lung tissue, from normal alveolar macrophages. An identical MMP9 sequence is found in granulocytes and in lung fibroblasts. The MMP2 sequence is derived from normal skin fibroblasts.

[0055] When the MMP9 and MMP2 structures are aligned on 148 residues with similar secondary structure or conformation, the average difference between equivalent alpha carbon atoms is 0.64 Å. The structures of MMP9 and MMP2 are therefore similar but significant differences occur in the S1′ specificity pocket. Residues 425-431 in MMP9 (427-433 for MMP2, numbered as for the intact MMP2 in Morgunova et al. 1999) form a loop which deviates from the equivalent loop in the MMP2 structures. The S1′ pocket in MMP9 and MMP2 may be described as a tunnel leading out to solvent, but the exact shape of the pocket in MMP9 is unique. Arg424 in MMP9 narrows the end of the S1′ pocket, pointing away from the pocket; the corresponding residue in MMP2 is a threonine (426).

[0056] According to a further aspect of the invention we provide a method to determine or design the three dimensional structure of a crystal form of MMP9 (including MMP9 mutants, variants, and co-complexes) by using a particular MMP9 catalytic domain structure. The atomic co-ordinates of a first MMP9 crystal may be used to model the structure of a second MMP9 crystal by difference Fourier or molecular replacement.

[0057] The term “molecular replacement” refers to a method that involves generating a preliminary model of a crystal whose atomic coordinates are not known, by orienting and positioning a related molecule whose atomic coordinates are known. Phases are then calculated from this model and combined with observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown.

[0058] The second crystal may be a crystal of a mutant, variant, or co-complex of MMP9. Preferably the active site binding region of the first MMP9 crystal is identical or equivalent to that defined by Tables 1 (amino acid residues) and Tables 2 or 3 (atomic coordinates). The shape of the MMP9 active site binding region in the second crystal model is an equivalent shape to that of the first. Equivalent shape is defined as a difference of up to 1.5 Å between each pair of matching Cα atoms for each residue contributing to the active site binding region. In other words, the positions of the Cα carbon atoms of the constituent residues of the active site binding region are within 1.5 Å when the first and second crystal structures are superposed.

[0059] So the invention provides a method to determine or design the three dimensional structure of a crystal form of MMP9 by difference Fourier or molecular replacement, using the atomic coordinates of a first MMP9 crystal to model the structure of a second MMP9 crystal wherein the active site binding region amino acid residues of the first MMP9 crystal are identical or equivalent to those listed in Table 1 and the shape of the active site binding region of the first MMP9 crystal is defined by the atomic coordinates given in Table 2 or Table 3 or by equivalent coordinates.

[0060] The method may be carried out as follows. An MMP9 protein (wild type, mutant or variant) is purified and crystallised as a pure protein or as a co-complex with an inhibitor compound. This crystal may have the same crystal form (same protein packing) as the crystal structure defined in Tables 2 or 3, or it may have a different crystal form (different protein packing). By taking some measurements of the crystal and using the atomic coordinates in Tables 2 or 3 (or equivalent coordinates), it is possible to work out the structure of the crystal by the known methods of difference Fourier (for the same packing) or molecular replacement (for different packing).

[0061] The invention further provides MMP9 proteins (including mutants and variants) designed by the above method. The MMP9 proteins may have identical properties to wild type MMP9 or may have one or more different properties compared to wild type MMP9 (for example, they may be more active mutants or inactive mutants).

[0062] According to a further aspect of the invention, we provide a method to select or design chemical modulators (preferably inhibitors) of MMP9 by using the MMP9 catalytic domain structure (including that of mutants, variants, and co-complexes) and the shape of the active site binding region (or an equivalent shape as previously defined). Information from the three dimensional atomic coordinates of the reverse hydroxamate inhibitor and its spatial orientation in relation to the three dimensional atomic coordinates of the MMP9 catalytic domain is used as a tool to design MMP9 modulators (preferably inhibitors). Small-molecule modulators of MMP9 may be selected or designed to fit into the shape of the active site binding region.

[0063] An MMP9 modulator may be selected by:

[0064] a) searching a structural database of compounds using parameters derived from the structure of the MMP9 active site binding region identical or equivalent to that defined by Tables 1 (amino acid residues) and Tables 2 or 3 (atomic coordinates); and

[0065] b) selecting a compound structure that may mimic or interact with these parameters.

[0066] It is then possible to synthesise the selected compound and test its activity.

[0067] An MMP9 modulator may be designed by taking parameters derived from the structure of the MMP9 active site binding region identical or equivalent to that defined by Tables 1 (amino acid residues) and Tables 2 or 3 (atomic coordinates) and using these parameters to model a compound structure that may mimic or interact with these parameters. The starting point for design may be the structure of a known weak inhibitor compound that can be modelled to an improved inhibitor compound using the MMP9 structural parameters. The designed compound may then be synthesised and tested.

[0068] The MMP9 mutant (E402Q) construct is a particularly useful tool for iterative drug design. Since the mutant protein is inactive, it can be stored in the absence of any inhibitor and subsequently be used for standard co-crystallisation procedures or crystal soaking procedures with both potent inhibitors and weaker binders.

[0069] Knowledge of the structural determinants that account for the difference in substrate specificity between MMP9 and MMP2 and other MMPs provides a foundation for the design of highly specific modulators of the MMP9 enzyme. Structural differences at the S1′ pocket between MMP9 and other MMPs (defined by differences in the atomic coordinates of residues in the S1′ pocket) may be used to design selective MMP9 modulators.

[0070] So the invention provides a method to select or design a chemical modulator of MMP9 by selecting or designing a modulator with a three dimensional structure that fits into the MMP9 active site binding region, wherein the active site binding region amino acid residues are identical or equivalent to those listed in Table 1 and the shape of the active site binding region is defined by the atomic coordinates given in Table 2 or Table 3 or by equivalent coordinates.

[0071] As described above, the MMP9 crystal structure may be used in the rational design of drugs which modulate (preferably inhibit) the action of MMP9. These MMP9 modulators may be used to prevent or treat the undesirable physical and pharmacological properties of MMP9 activity.

[0072] The invention provides modulators of MMP9 selected or designed by the above method. These modulators particularly inhibitors) may be useful as therapeutic agents to treat undesirable properties of MMP9 activity in humans.

[0073] Therefore in a further aspect, the present invention provides a modulator of MMP9 selected or designed by the above method or a pharmaceutically acceptable salt or in vivo hydrolysable ester thereof suitable for use in a method of therapeutic treatment of the human or animal body. In particular we disclose use in the treatment of a disease or condition mediated by MMP9.

[0074] In yet a further aspect the present invention provides a method of treating a metalloproteinase mediated disease or condition which comprises administering to a warm-blooded animal a therapeutically effective amount of a modulator of MMP9 or a pharmaceutically acceptable salt or in vivo hydrolysable ester thereof. The modulator of MMP 9 is selected or designed by the method described above. Metalloproteinase mediated diseases or conditions include: tumour growth and metastasis in cancer, inflammatory diseases in general, such as arthritis and osteoarthritis; atherosclerosis; aneurysmal disease; ventricular remodelling and heart failure; restenosis; periodontitis; neurodegenerative and neuroinflammatory diseases such as multiple sclerosis and Guillain Barré Syndrome; glomerulonephritis; blood-brain barrier leakage; breakdown in stroke and meningitis; occular autoimmune disease such as uveoretinitis; graft-versus-host disease; and non-insulin-dependant diabetes.

[0075] The present invention will now be described with reference to the following non-limiting Examples.

EXAMPLE 1

[0076] Production of the Catalytic Domain of MMP9

[0077] The catalytic domain of human MMP9 was cloned so that the fibronectin type II-like domains which occur as an insert within the catalytic domain sequence were deleted (Shipley et al 1996). The remaining catalytic domain fragment containing residues 107-216 was fused to residues 391-443 by overlapping PCR The 5′ primer introduced an ATG start codon directly upstream of the phenylalanine (107) and a stop codon was introduced, via the 3′ primer, after residue 443 to prevent translation of the hemopexin-like domains. An inactive mutant of this domain was created by site directed mutagenesis, such that the glutamate (GAG) at position 402 of the full-length CDNA was mutated to give a glutamine (CAG). The product was cloned into the Ndel and Xhol sites of a T7 expression vector and transformed into E. coli BL21(DE3).This was grown up to log phase and induced with 0.4 mM IPTG for 4 hours to express the 18 kDa MMP9 catalytic domain protein

[0078] Following expression in E. coli, MMP9(107-216,391-443) is mainly located in the inclusion body fraction. The E. coli were harvested, washed and lysed and centrifuged to isolate the insoluble protein. The insoluble fraction was then suspended in 6M Urea to solubilise the protein. To generate active MMP9(107-216,391-443) the solubilised material was dialysed sequentially versus 4M, 1M and 0M Urea. Crystallization of this material after purification resulted in disordered crystals and analysis of the protein using mass spectrometry indicated heterogeneity at the N-terminus. It was found that the addition of acetohydroxamic acid in the refold buffers inhibited auto-proteolysis of the N-terminus of the protein. When crystallization of the protein was carried out it was found that where no acetohydroxamic acid was added during refolding disordered crystals formed whereas when acetohydroxamic was added the crystals were well ordered. Post dialysis, the protein was subjected to zinc chelate chromatography which selectively bound the MMP9 catalytic domain. A further chromatography step was then carried out using the tripeptide Pro-Leu-Gly bound to sepharose which bound correctly folded MMP9 catalytic domain. The protein was then eluted by addition of an MMP9 inhibitor. Expression and refolding of the [E402Q]MMP9(107-216,391-443) construct was carried out as for the wild type construct except that no acetohydroxamic acid was added to the refold buffers. After refolding, the enzyme was purified via zinc chelate chromatography followed by a gel filtration step.

EXAMPLE 2

[0079] Purification of MMP9 Catalytic Domain

[0080] This method involves first the dialysis of inclusion bodies versus 4M, 2M, 1M and 0M Urea to generate active enzyme. The P9(107-216,391-443) present is then separated from impurities by zinc chelate chromatography on a Chelating Sepharose Fast Flow chromatography column charged with 0.1M zinc acetate. Further purification is then carried out by binding MMP9(107-216,391-443) to an NHS Activated Sepharose chromatography column bound with the peptide Pro-Leu-Gly. The MMP9(107-216,391-443) present is eluted by the addition of 0.5 mM MMMP9 Inhibitor. Mass spectrometry and N-terminal sequencing indicate the product to be MMP9(107-216,391-443) with an extra Met at the N-termini. The product is shown to possess MMP activity via-FRET and Zymographic analysis. Post refolding, the mutated enzyme was purified via zinc chelate chromatography followed by a gel filtration step.

EXAMPLE 3

[0081] Crystallisation of MMP9 Catalytic Domain

[0082] The MMP9:reverse hydroxamate inhibitor complexes were crystallised at 15° C. by hanging-drop vapour diffusion. For crystallization of the wild type complex, the enzyme-inhibitor complex was purified as detailed above. The crystallisation drops contained a 1:1 mixture of purified complex solution (0.55 mg/ml protein and 0.5 mM inhibitor solution concentrated to ˜4 mg/ml in 20 mM Tris-HCl pH 7.5, 2 mM CaCl₂, 50 mM NaCl) and reservoir buffer (3.6M NaCl, 0.1M Hepes pH 7.5). For crystallisation of the mutant complex, the protein was concentrated to 4 mg/ml solution (in 20 mM Tris-HCl pH 7.5, 50 mM NaCl), 5 mM inhibitor was then added to this solution and the complex was incubated on ice for 30 minutes prior to setting up crystallisation trials. The drops contained a 1:1 mixture of complex solution and reservoir buffer (2.6-2.8M NaCl, 0.1M Hepes pH 9.0). The wild type and mutant crystals are isomorphous and belong to space group P4₁2₁2 with unit cell dimensions a=b=56 Å and c=263 Å, and contain two molecules per crystal asymmetric unit. The term “space group” refers to the arrangement of symmetry elements within a unit cell.

EXAMPLE 4

[0083] Determination of the Three dimensional Structure of the Catalytic Domain of MMP9

[0084] Three dimensional diffraction data extending to a resolution of 2.3 Å (2.1 Å for the mutant) were collected at the Synchrotron Radiation Source, Daresbury, UK (station 9.6; wavelength 0.87 Å). Data were collected with an ADSC CCD detector at room temperature from more than one crystal. These images were evaluated using the MOSFLM4 software package. The CCP4 suite of programs was used for the data reduction and subsequent data handling. 77,726 observations of 17,375 unique reflections were merged with an R-factor of 11.7% (mutant data: 50,609 observations of 18,841 unique reflections were merged with an R-factor of 14.7%). The wild type structure was solved by molecular replacement, using the program AMoRe and a model based on PDB entry 1HFS, the structure of uninhibited stromelysin. The current model was constructed by interactive model building using the program Quanta98 and refined using X-PLOR. In the early stages of model building, real-space averaging using RAVE significantly improved the quality of electron density maps. The current model of the wild type catalytic domain was inspected against electron density maps and comprises 159 (156, molecule 2) out of 163 residues; 2 Zn2+ and 5 Ca2+ ions; 1 inhibitor and 54 water molecules per subunit. The omitted residues are at the N-terminus. Residue Arg424 has only weak electron density beyond the Cδ atom (Cβ in the second molecule in the crystal asymmetric unit). The R-factor of the refined model is 22.1% (Rfree=26.9%) and the stereo-chemistry is reasonable (r.m.s. deviation of bonds=0.011, angles=1.5). The mutant structure was determined by molecular replacement using the refined wild type structure as trial model. The current model of the mutant was constructed by interactive model building using the program Quanta98 and refined using CNX. The current model of the mutated catalytic domain was inspected against electron density maps and comprises 159 (155, subunit 2) out of 163 residues; 2 Zn2+ and 5 Ca2+ ions; 1 inhibitor and 90 water molecules per subunit. The omitted residues are at the N-terminus. Residue Arg424 has only weak electron density beyond the Cδ atom (Cβ in subunit 2). The R-factor of the refined model is 21.3% (Rfree=25.8%) and the stereo-chemistry is reasonable (r.m.s. deviation of bonds=0.006, angles=1.1).). The R-factor of the refined mutant model is 21.3% (Rfree=25.8%) and the stereo-chemistry is reasonable (r.m.s. deviation of bonds=0.006, angles=1.1).

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[0134] Zhang, X. et al. J. Mol. Biol. 301, 513-524 (2000). TABLE 2 Three dimensional atomic coordinates of the wild type MMP9 construct in complex with the reverse hydroxamate compound of Formula I. REMARK coordinates from restrained individual B-factor refinement REMARK refinement resolution: 100 - 2.3 A REMARK starting r= 0.2096 free_r= 0.2397 REMARK final r= 0.2074 free_r= 0.2408 REMARK B rmsd for bonded mainchain atoms= 1.707 target= 1.5 REMARK B rmsd for bonded sidechain atoms= 2.673 target= 2.0 REMARK B rmsd for angle mainchain atoms= 2.714 target= 2.0 REMARK B rmsd for angle sidechain atoms= 3.856 target= 2.5 REMARK wa= 2.19316 REMARK rweight=5.978512E-02 REMARK target= mlf steps= 30 REMARK sg= P4(1)2(1)2 a= 56.005 b= 56.005 c= 262.655 alpha= 90 beta= 90 gamma= 9 REMARK parameter file 1 : MSI_CNX_TOPPAR:protein_rep.param REMARK parameter file 2 : MSI_CNX_TOPPAR:ion.param REMARK parameter file 3 : MSI_CNX_TOPPAR:water_rep.param REMARK parameter file 4 : fra.par REMARK molecular structure file: mmp9.mtf REMARK input coordinates: anneal_restrain_1.pdb REMARK reflection file= mmp9_rf.hkl REMARK ncs= restrain ncs file= ncs_restrain.def REMARK B-correction resolution: 6.0 - 2.3 REMARK initial B-factor correction applied to fobs: REMARK B11= −4.644 B22= −4.644 B33= 9.288 REMARK B12= 0.000 B13= 0.000 B23= 0.000 REMARK B-factor correction applied to coordinate array B: 0.533 REMARK bulk solvent: (Mask) density level= 0.372729 e/A{circumflex over ( )}3, B-factor 48.8354 A{circumflex over ( )}2 REMARK reflections with |Fobs|/sigma_F < 0.0 rejected REMARK reflections with |Fobs|>1000 * rms(Fobs) rejected REMARK theoretical total number of refl. in resol. range: 19670 (100.0%) REMARK number of unobserved reflections (no entry or |F|=0): 2295 (11.7%) REMARK number of reflections rejected: 0(0.0%) REMARK total number of reflections used: 17375 (88.3%) REMARK number of reflections in working set: 16691 (84.9%) REMARK number of reflections in test set: 684 (3.5%) REMARK FILENAME=“bindividual7.pdb” REMARK DATE:Nov-30-2000 13:59:53 created by user: sian REMARK Written by CNX VERSION:2000 CRYST1 56.005 56.005 262.655 90.00 90.00 90.00 P 41 21 2 SCALE1 0.017856 0.000000 0.000000 0.00000 SCALE2 0.000000 0.017856 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003807 0.00000 ATOM 1 CB PHE A 110 68.144 27.293 107.042 1.00 76.67 A C ATOM 2 CG PHE A 110 69.059 26.231 107.577 1.00 76.83 A C ATOM 3 CD1 PHE A 110 70.433 26.309 107.372 1.00 76.63 A C ATOM 4 CD2 PHE A 110 68.547 25.145 108.276 1.00 76.62 A C ATOM 5 CE1 PHE A 110 71.282 25.322 107.853 1.00 75.40 A C ATOM 6 CB2 PHE A 110 69.390 24.152 108.763 1.00 76.11 A C ATOM 7 CZ PHE A 110 70.760 24.241 108.550 1.00 75.74 A C ATOM 8 C PHE A 110 67.022 28.261 105.029 1.00 76.18 A C ATOM 9 O PHE A 110 65.965 28.280 105.664 1.00 76.86 A O ATOM 10 N PHE A 110 69.510 28.084 105.133 1.00 76.75 A N ATOM 11 CA PHE A 110 68.217 27.455 105.522 1.00 76.45 A C ATOM 12 N GLU A 111 67.204 28.928 103.893 1.00 74.63 A N ATOM 13 CA GLU A 111 66.148 29.724 103.279 1.00 73.01 A C ATOM 14 CB GLU A 111 66.490 31.215 103.335 1.00 75.82 A C ATOM 15 CG GLU A 111 66.819 31.745 104.726 1.00 80.41 A C ATOM 16 CD GLU A 111 65.689 31.554 105.725 1.00 83.58 A C ATOM 17 OE1 GLU A 111 64.561 32.022 105.452 1.00 85.28 A O ATOM 18 OE2 GLU A 111 65.934 30.941 106.789 1.00 84.02 A 0 ATOM 19 C GLU A 111 66.025 29.282 101.826 1.00 69.95 A C ATOM 20 O GLU A 111 67.025 29.180 101.111 1.00 70.43 A 0 ATOM 21 N GLY A 112 64.801 29.009 101.394 1.00 66.03 A N ATOM 22 CA GLY A 112 64.587 28.577 100.027 1.00 60.34 A C ATOM 23 C GLY A 112 63.299 29.143 99.479 1.00 56.89 A C ATOM 24 O GLY A 112 62.515 29.744 100.213 1.00 57.97 A 0 ATOM 25 N ASP A 113 63.077 28.955 98.185 1.00 53.94 A N ATOM 26 CA ASP A 113 61.866 29.459 97.553 1.00 50.40 A C ATOM 27 CB ASP A 113 62.209 30.556 96.543 1.00 52.58 A C ATOM 28 CG ASP A 113 62.790 31.792 97.202 1.00 53.44 A C ATOM 29 OD1 ASP A 113 62.092 32.405 98.039 1.00 53.76 A 0 ATOM 30 OD2 ASP A 113 63.944 32.146 96.885 1.00 53.72 A 0 ATOM 31 C ASP A 113 61.098 28.345 96.867 1.00 46.20 A C ATOM 32 O ASP A 113 60.589 28.519 95.763 1.00 46.06 A 0 ATOM 33 N LEU A 114 61.024 27.198 97.535 1.00 40.51 A N ATOM 34 CA LEU A 114 60.309 26.043 97.018 1.00 35.29 A C ATOM 35 CB LEU A 114 61.265 24.870 96.812 1.00 35.18 A C ATOM 36 CG LEU A 114 62.424 25.022 95.829 1.00 35.74 A C ATOM 37 CD1 LEU A 114 63.155 23.689 95.726 1.00 34.64 A C ATOM 38 CD2 LEU A 114 61.906 25.455 94.463 1.00 31.83 A C ATOM 39 C LEU A 114 59.229 25.624 98.003 1.00 33.60 A C ATOM 40 O LEU A 114 59.363 25.842 99.205 1.00 33.68 A 0 ATOM 41 N LYS A 115 58.151 25.040 97.489 1.00 30.09 A N ATOM 42 CA LYS A 115 57.066 24.556 98.331 1.00 28.79 A C ATOM 43 CB LYS A 115 55.782 25.350 98.091 1.00 27.23 A C ATOM 44 CG LYS A 115 55.136 25.113 96.739 1.00 30.27 A C ATOM 45 CD LYS A 115 53.726 25.671 96.711 1.00 31.99 A C ATOM 46 CE LYS A 115 53.015 25.309 95.420 1.00 33.32 A C ATOM 47 NZ LYS A 115 51.602 25.772 95.434 1.00 31.74 A N ATOM 48 C LYS A 115 56.854 23.099 97.946 1.00 27.74 A C ATOM 49 o LYS A 115 57.490 22.610 97.017 1.00 26.52 A O ATOM 50 N TRP A 116 55.984 22.398 98.660 1.00 26.86 A N ATOM 51 CA TRP A 116 55.725 21.005 98.327 1.00 26.50 A C ATOM 52 CB TRP A 116 55.139 20.242 99.525 1.00 24.26 A C ATOM 53 CG TRP A 116 56.071 20.142 100.708 1.00 26.96 A C ATOM 54 CD2 TRP A 116 57.243 19.321 100.810 1.00 26.47 A C ATOM 55 CE2 TRP A 116 57.806 19.554 102.087 1.00 25.23 A C ATOM 56 CE3 TRP A 116 57.873 18.414 99.946 1.00 25.47 A C ATOM 57 CD1 TRP A 116 55.977 20.821 101.894 1.00 23.47 A C ATOM 58 NE1 TRP A 116 57.014 20.472 102.724 1.00 22.33 A N ATOM 59 CZ2 TRP A 116 58.972 18.910 102.521 1.00 24.08 A C ATOM 60 CZ3 TRP A 116 59.037 17.774 100.378 1.00 24.64 A C ATOM 61 CH2 TRP A 116 59.572 18.027 101.654 1.00 25.34 A C ATOM 62 C TRP A 116 54.723 20.991 97.184 1.00 27.50 A C ATOM 63 O TRP A 116 53.828 21.836 97.125 1.00 25.79 A O ATOM 64 N HIS A 117 54.877 20.039 96.271 1.00 27.87 A N ATOM 65 CA HIS A 117 53.950 19.932 95.158 1.00 29.48 A C ATOM 66 CB HIS A 117 54.692 19.528 93.885 1.00 25.71 A C ATOM 67 CG HIS A 117 55.384 20.674 93.214 1.00 27.00 A C ATOM 68 CD2 HIS A 117 55.394 21.998 93.501 1.00 27.93 A C ATOM 69 ND1 HIS A 117 56.184 20.520 92.103 1.00 28.15 A N ATOM 70 CE1 HIS A 117 56.659 21.697 91.736 1.00 25.56 A C ATOM 71 NE2 HIS A 117 56.195 22.611 92.568 1.00 25.76 A N ATOM 72 C HIS A 117 52.794 18.982 95.465 1.00 31.31 A C ATOM 73 O HIS A 117 51.849 18.873 94.687 1.00 36.62 A O ATOM 74 N HIS A 118 52.868 18.292 96.600 1.00 28.91 A N ATOM 75 CA HIS A 118 51.782 17.412 97.007 1.00 27.75 A C ATOM 76 CB HIS A 118 52.257 15.966 97.160 1.00 26.46 A C ATOM 77 CG HIS A 118 53.454 15.800 98.041 1.00 28.06 A C ATOM 78 CD2 HIS A 118 53.587 15.230 99.262 1.00 26.27 A C ATOM 79 ND1 HIS A 118 54.715 16.213 97.672 1.00 27.31 A N ATOM 80 CE1 HIS A 118 55.575 15.901 98.625 1.00 25.21 A C ATOM 81 NE2 HIS A 118 54.916 15.304 99.600 1.00 25.44 A N ATOM 82 C HIS A 118 51.232 17.949 98.322 1.00 28.02 A C ATOM 83 O HIS A 118 51.906 18.717 99.006 1.00 30.48 A O ATOM 84 N HIS A 119 50.008 17.566 98.670 1.00 28.21 A N ATOM 85 CA HIS A 119 49.394 18.049 99.900 1.00 28.31 A C ATOM 86 CB HIS A 119 48.001 18.597 99.607 1.00 27.88 A C ATOM 87 CG HIS A 119 48.015 19.881 98.843 1.00 30.03 A C ATOM 88 CD2 HIS A 119 49.045 20.642 98.402 1.00 28.56 A C ATOM 89 ND1 HIS A 119 46.862 20.530 98.452 1.00 32.34 A N ATOM 90 CE1 HIS A 119 47.182 21.636 97.804 1.00 30.91 A C ATOM 91 NE2 HIS A 119 48.500 21.728 97.760 1.00 30.11 A N ATOM 92 C HIS A 119 49.318 17.040 101.034 1.00 28.11 A C ATOM 93 O HIS A 119 49.120 17.424 102.184 1.00 28.79 A O ATOM 94 N ASN A 120 49.447 15.757 100.715 1.00 28.28. A N ATOM 95 CA ASN A 120 49.418 14.724 101.742 1.00 30.67 A C ATOM 96 CE ASN A 120 48.753 13.442 101.206 1.00 35.59 A C ATOM 97 CG ASN A 120 49.339 12.970 99.874 1.00 40.97 A C ATOM 98 OD1 ASN A 120 49.628 13.776 98.982 1.00 42.91 A O ATOM 99 ND2 ASN A 120 49.494 11.652 99.728 1.00 42.68 A N ATOM 100 C ASN A 120 50.873 14.489 102.141 1.00 29.30 A C ATOM 101 O ASN A 120 51.564 13.634 101.585 1.00 29.67 A O ATOM 102 N ILE A 121 51.330 15.287 103.103 1.00 26.98 A N ATOM 103 CA ILE A 121 52.710 15.233 103.577 1.00 26.04 A C ATOM 104 CE ILE A 121 53.138 16.617 104.109 1.00 26.73 A C ATOM 105 CG2 ILE A 121 54.574 16.568 104.626 1.00 26.58 A C ATOM 106 CG1 ILE A 121 52.997 17.650 102.987 1.00 29.00 A C ATOM 107 CD1 ILE A 121 53.451 19.037 103.357 1.00 32.81 A C ATOM 108 C ILE A 121 52.945 14.179 104.650 1.00 23.95 A C ATOM 109 O ILE A 121 52.081 13.928 105.484 1.00 24.37 A O ATOM 110 N THR A 122 54.119 13.560 104.621 1.00 20.08 A N ATOM 111 CA THR A 122 54.441 12.534 105.598 1.00 21.17 A C ATOM 112 CB THR A 122 54.763 11.172 104.914 1.00 22.42 A C ATOM 113 OG1 THR A 122 55.948 11.294 104.115 1.00 20.53 A O ATOM 114 CG2 THR A 122 53.592 10.722 104.042 1.00 21.00 A C ATOM 115 C THR A 122 55.624 12.925 106.481 1.00 20.68 A C ATOM 116 O THR A 122 56.502 13.706 106.081 1.00 18.28 A O ATOM 117 N TYR A 123 55.640 12.382 107.693 1.00 18.69 A N ATOM 118 CA TYR A 123 56.728 12.671 108.612 1.00 17.02 A C ATOM 119 CB TYR A 123 56.374 13.828 109.561 1.00 12.64 A C ATOM 120 CG TYR A 123 55.291 13.533 110.579 1.00 14.99 A C ATOM 121 CD1 TYR A 123 53.949 13.737 110.277 1.00 15.83 A C ATOM 122 CE1 TYR A 123 52.953 13.517 111.228 1.00 14.44 A C ATOM 123 CD2 TYR A 123 55.613 13.088 111.867 1.00 15.15 A C ATOM 124 CE2 TYR A 123 54.623 12.866 112.821 1.00 13.15 A C ATOM 125 CZ TYR A 123 53.296 13.087 112.495 1.00 14.54 A C ATOM 126 OH TYR A 123 52.305 12.912 113.439 1.00 17.15. A O ATOM 127 C TYR A 123 57.109 11.446 109.419 1.00 15.63 A C ATOM 128 O TYR A 123 56.277 10.594 109.735 1.00 14.88 A O ATOM 129 N TRP A 124 58.387 11.380 109.745 1.00 14.30 A N ATOM 130 CA TRP A 124 58.933 10.288 110.504 1.00 15.16 A C ATOM 131 CB TRP A 124 59.876 9.486 109.603 1.00 17.22 A C ATOM 132 CG TRP A 124 60.649 8.390 110.274 1.00 14.19 A C ATOM 133 CD2 TRP A 124 62.005 8.019 110.004 1.00 17.22 A C ATOM 134 CE2 TRP A 124 62.299 6.892 110.807 1.00 18.18 A C ATOM 135 CE3 TRP A 124 63.002 8.525 109.157 1.00 17.93 A C ATOM 136 CD1 TRP A 124 60.186 7.506 111.204 1.00 15.79 A C ATOM 137 NE1 TRP A 124 61.172 6.599 111.530 1.00 17.60 A N ATOM 138 CZ2 TRP A 124 63.548 6.262 110.788 1.00 17.69 A C ATOM 139 CZ3 TRP A 124 64.244 7.899 109.139 1.00 22.22 A C ATOM 140 CH2 TRP A 124 64.505 6.776 109.951 1.00 19.94 A C ATOM 141 C TRP A 124 59.679 10.321 111.720 1.00 15.01 A C ATOM 142 O TRP A 124 60.575 11.645 111.590 1.00 15.43 A O ATOM 143 N ILE A 125 59.283 10.365 112.903 1.00 13.81 A N ATOM 144 CA ILE A 125 59.960 10.754 114.127 1.00 14.20 A C ATOM 145 CB ILE A 125 59.009 10.697 115.341 1.00 14.44 A C ATOM 146 CG2 ILE A 125 59.758 11.087 116.609 1.00 10.36 A C ATOM 147 CG1 ILE A 125 57.833 11.649 115.110 1.00 14.53 A C ATOM 148 CD1 ILE A 125 56.721 11.500 116.106 1.00 16.01 A C ATOM 149 C ILE A 125 61.033 9.685 114.249 1.00 14.73 A C ATOM 150 O ILE A 125 60.763 8.564 114.660 1.00 17.21 A O ATOM 151 N GLN A 126 62.259 10.036 113.863 1.00 15.17 A N ATOM 152 CA GLN A 126 63.374 9.102 113.877 1.00 17.19 A C ATOM 153 CB GLN A 126 64.540 9.679 113.065 1.00 15.71 A C ATOM 154 CG GLN A 126 65.810 8.849 113.134 1.00 19.08 A C ATOM 155 CD GLN A 126 67.006 9.537 112.492 1.00 21.76 A C ATOM 156 OE1 GLN A 126 63.141 9.434 112.978 1.00 21.48 A O ATOM 157 NE2 GLN A 126 66.762 10.235 111.395 1.00 21.97 A N ATOM 158 C GLN A 126 63.858 3.702 115.270 1.00 18.20 A C ATOM 159 O GLN A 126 64.062 7.519 115.536 1.00 18.29 A O ATOM 160 N ASN A 127 64.066 9.681 116.145 1.00 19.88 A N ATOM 161 CA ASN A 127 64.515 9.397 117.504 1.00 18.22 A C ATOM 162 CB ASN A 127 66.042 9.423 117.594 1.00 19.01 A C ATOM 163 CG ASN A 127 66.631 10.770 117.242 1.00 21.39 A C ATOM 164 OD1 ASN A 127 65.957 11.798 117.310 1.00 25.90 A O ATOM 165 ND2 ASN A 127 67.909 10.774 116.880 1.00 20.17 A N ATOM 166 C ASN A 127 63.900 10.336 118.483 1.00 19.18 A C ATOM 167 O ASN A 127 63.238 11.341 118.068 1.00 18.72 A O ATOM 168 N TYR A 128 64.128 10.163 119.779 1.00 17.90 A N ATOM 169 CA TYR A 128 63.539 11.006 120.822 1.00 15.61 A C ATOM 170 CB TYR A 128 62.592 10.166 121.693 1.00 15.35 A C ATOM 171 CG TYR A 128 61.389 9.623 120.957 1.00 14.14 A C ATOM 172 CD1 TYR A 128 61.476 8.467 120.178 1.00 121.53 A C ATOM 173 CE1 TYR A 128 60.374 8.000 119.469 1.00 12.28 A C ATOM 174 CD2 TYR A 128 60.172 10.293 121.008 1.00 12.14 A C ATOM 175 CE2 TYR A 128 59.078 9.839 120.306 1.00 14.27 A C ATOM 176 CZ TYR A 128 59.182 8.698 119.539 1.00 13.46 A C ATOM 177 OH TYR A 128 58.084 8.292 118.837 1.00 12.04 A O ATOM 178 C TYR A 128 64.501 11.716 121.746 1.00 14.76 A C ATOM 179 O TYR A 128 65.681 11.396 121.808 1.00 15.87 A O ATOM 180 N SER A 129 63.969 12.693 122.471 1.00 17.19 A N ATOM 181 CA SER A 129 64.742 13.430 123.460 1.00 19.66 A C ATOM 182 CB SER A 129 64.173 14.826 123.675 1.00 17.51 A C ATOM 183 OG SER A 129 64.731 15.394 124.844 1.00 16.48 A O ATOM 184 C SER A 129 64.600 12.640 124.753 1.00 22.10 A C ATOM 185 O SER A 129 63.646 11.882 124.920 1.00 21.65 A O ATOM 186 N GLU A 130 65.529 12.821 125.677 1.00 24.54 A N ATOM 187 CA GLU A 130 65.459 12.085 126.925 1.00 28.04 A C ATOM 188 CB GLU A 130 66.884 11.859 127.459 1.00 31.45 A C ATOM 189 CG GLU A 130 67.799 11.117 126.464 1.00 36.20 A C ATOM 190 CD GLU A 130 69.207 10.871 126.996 1.00 37.68 A C ATOM 191 OE1 GLU A 130 69.330 10.501 128.182 1.00 43.10 A O ATOM 192 OE2 GLU A 130 70.189 11.031 126.237 1.00 32.89 A O ATOM 193 C GLU A 130 64.587 12.788 127.971 1.00 27.09 A C ATOM 194 O GLU A 130 64.154 12.167 128.939 1.00 29.20 A O ATOM 195 N ASP A 131 64.301 14.069 127.751 1.00 23.80 A N ATOM 196 CA ASP A 131 63.519 14.870 128.693 1.00 21.55 A C ATOM 197 CB ASP A 131 63.657 16.355 128.367 1.00 20.53 A C ATOM 198 CG ASP A 131 65.084 16.774 128.149 1.00 21.96 A C ATOM 199 OD1 ASP A 131 65.993 16.132 128.718 1.00 23.79 A O ATOM 200 OD2 ASP A 131 65.291 17.760 127.417 1.00 19.14 A O ATOM 201 C ASP A 131 62.029 14.589 128.821 1.00 22.60 A C ATOM 202 O ASP A 131 61.417 14.946 129.826 1.00 22.01 A O ATOM 203 N LEU A 132 61.426 13.985 127.808 1.00 21.60 A N ATOM 204 CA LEU A 132 59.996 13.736 127.862 1.00 17.46 A C ATOM 205 CB LEU A 132 59.274 14.744 126.964 1.00 18.77 A C ATOM 206 CG LEU A 132 59.410 16.228 127.329 1.00 16.38 A C ATOM 207 CD1 LEU A 132 58.952 17.103 126.185 1.00 16.14 A C ATOM 208 CD2 LEU A 132 58.584 16.513 128.574 1.00 17.73 A C ATOM 209 C LEU A 132 59.625 12.322 127.447 1.00 17.91 A C ATOM 210 O LEU A 132 60.350 11.668 126.703 1.00 20.57 A O ATOM 211 N PRO A 133 58.493 11.818 127.952 1.00 18.54 A N ATOM 212 CD PRO A 133 57.590 12.397 128.962 1.00 16.46 A C ATOM 213 CA PRO A 133 58.070 10.464 127.588 1.00 18.30 A C ATOM 214 CB PRO A 133 56.828 10.250 128.448 1.00 16.44 A C ATOM 215 CG PRO A 133 57.029 11.174 129.599 1.00 13.96 A C ATOM 216 C PRO A 133 57.739 10.482 126.092 1.00 18.28 A C ATOM 217 O PRO A 133 57.305 11.511 125.566 1.00 15.16 A O ATOM 218 N ARG A 134 57.931 9.358 125.412 1.00 18.49 A N ATOM 219 CA ARG A 134 57.661 9.313 123.978 1.00 20.66 A C ATOM 220 CB ARG A 134 58.084 7.961 123.411 1.00 20.98 A C ATOM 221 CG ARG A 134 59.563 7.723 123.628 1.00 21.85 A C ATOM 222 CD ARG A 134 60.064 6.476 122.953 1.00 25.93 A C ATOM 223 NE ARG A 134 61.506 6.346 123.137 1.00 29.18 A N ATOM 224 CZ ARG A 134 62.234 5.347 122.652 1.00 32.95 A C ATOM 225 NH1 ARG A 134 61.649 4.384 121.949 1.00 31.93 A N ATOM 226 NH2 ARG A 134 63.544 5.314 122.867 1.00 31.66 A N ATOM 227 C ARG A 134 56.217 9.633 123.615 1.00 20.30 A C ATOM 228 O ARG A 134 55.961 10.226 122.575 1.00 19.91 A O ATOM 229 N ALA A 135 55.274 9.256 124.470 1.00 19.00 A N ATOM 230 CA ALA A 135 53.871 9.552 124.201 1.00 20.03 A C ATOM 231 CB ALA A 135 52.980 8.861 125.237 1.00 18.70 A C ATOM 232 C ALA A 135 53.642 11.073 124.226 1.00 19.99 A C ATOM 233 O ALA A 135 52.814 11.601 123.489 1.00 19.37 A O ATOM 234 N VAL A 136 54.378 11.774 125.082 1.00 18.65 A N ATOM 235 CA VAL A 136 54.245 13.227 125.175 1.00 18.87 A C ATOM 236 CB VAL A 136 54.950 13.777 126.459 1.00 18.18 A C ATOM 237 CG1 VAL A 136 54.999 15.309 126.443 1.00 16.50 A C ATOM 238 CG2 VAL A 136 54.204 13.303 127.688 1.00 13.02 A C ATOM 239 C VAL A 136 54.838 13.900 123.930 1.00 17.85 A C ATOM 240 O VAL A 136 54.277 14.870 123.400 1.00 16.07 A O ATOM 241 N ILE A 137 55.969 13.374 123.469 1.00 14.93 A N ATOM 242 CA ILE A 137 56.630 13.916 122.295 1.00 13.94 A C ATOM 243 CB ILE A 137 58.035 13.292 122.121 1.00 13.55 A C ATOM 244 CG2 ILE A 137 58.657 13.730 120.789 1.00 10.34 A C ATOM 245 CG1 ILE A 137 58.917 13.705 123.307 1.00 11.84 A C ATOM 246 CD1 ILE A 137 60.329 13.165 123.274 1.00 8.78 A C ATOM 247 C ILE A 137 55.781 13.689 121.044 1.00 13.89 A C ATOM 248 O ILE A 137 55.557 14.616 120.270 1.00 13.43 A O ATOM 249 N ASP A 138 55.298 12.465 120.850 1.00 14.79 A N ATOM 250 CA ASP A 138 54.469 12.168 119.685 1.00 16.05 A C ATOM 251 CB ASP A 138 53.891 10.748 119.764 1.00 14.50 A C ATOM 252 CG ASP A 138 54.946 9.662 119.593 1.00 16.77 A C ATOM 253 OD1 ASP A 138 56.089 9.967 119.188 1.00 18.40 A O ATOM 254 OD2 ASP A 138 54.619 8.484 119.853 1.00 20.23 A O ATOM 255 C ASP A 138 53.317 13.170 119.602 1.00 16.70 A C ATOM 256 O ASP A 138 53.086 13.784 118.564 1.00 19.57 A O ATOM 257 N ASP A 139 52.612 13.337 120.716 1.00 16.62 A N ATOM 258 CA ASP A 139 51.460 14.232 120.801 1.00 15.09 A C ATOM 259 CB ASP A 139 50.812 14.099 122.181 1.00 14.62 A C ATOM 260 CG ASP A 139 49.611 15.003 122.354 1.00 16.52 A C ATOM 261 OD1 ASP A 139 48.584 14.769 121.692 1.00 19.96 A O ATOM 262 OD2 ASP A 139 49.688 15.953 123.152 1.00 12.35 A O ATOM 263 C ASP A 139 51.785 15.693 120.526 1.00 15.75 A C ATOM 264 O ASP A 139 51.004 16.396 119.894 1.00 17.52 A O ATOM 265 N ALA A 140 52.935 16.152 121.008 1.00 16.49 A N ATOM 266 CA ALA A 140 53.356 17.536 120.805 1.00 14.14 A C ATOM 267 CB ALA A 140 54.648 17.819 121.586 1.00 10.53 A C ATOM 268 C ALA A 140 53.576 17.805 119.319 1.00 13.23 A C ATOM 269 O ALA A 140 53.156 18.838 118.797 1.00 13.50 A O ATOM 270 N PHE A 141 54.249 16.877 118.645 1.00 12.36 A N ATOM 271 CA PHE A 141 54.501 17.017 117.216 1.00 15.20 A C ATOM 272 CB PHE A 141 55.431 15.901 116.722 1.00 13.79 A C ATOM 273 CG PHE A 141 56.867 16.073 117.146 1.00 11.40 A C ATOM 274 CD1 PHE A 141 57.408 17.340 117.318 1.00 12.07 A C ATOM 275 CD2 PHE A 141 57.685 14.973 117.341 1.00 11.50 A C ATOM 276 CE1 PHE A 141 58.752 17.507 117.678 1.00 15.23 A C ATOM 277 CE2 PHE A 141 59.032 15.133 117.701 1.00 10.84 A C ATOM 278 CZ PHE A 141 59.564 16.396 117.868 1.00 9.69 A C ATOM 279 C PHE A 141 53.183 16.988 116.433 1.00 15.88 A C ATOM 280 O PHE A 141 52.980 17.783 115.516 1.00 18.45 A O ATOM 281 N ALA A 142 52.289 16.080 116.815 1.00 15.46 A N ATOM 282 CA ALA A 142 50.997 15.940 116.156 1.00 16.51 A C ATOM 283 CB ALA A 142 50.235 14.769 116.751 1.00 16.42 A C ATOM 284 C ALA A 142 50.175 17.217 116.281 1.00 17.88 A C ATOM 285 O ALA A 142 49.519 17.642 115.327 1.00 14.95 A O ATOM 286 N ARG A 143 50.207 17.826 117.464 1.00 17.58 A N ATOM 287 CA ARG A 143 49.465 19.055 117.687 1.00 16.25 A C ATOM 288 CB ARG A 143 49.349 19.353 119.191 1.00 13.94 A C ATOM 289 CC ARG A 143 48.421 18.387 119.930 1.00 13.87 A C ATOM 290 CD ARG A 143 48.231 18.747 121.404 1.00 13.42 A C ATOM 291 NE ARG A 143 49.470 18.634 122.168 1.00 12.17 A N ATOM 292 CZ ARG A 143 50.164 19.671 122.631 1.00 14.73 A C ATOM 293 NH1 ARG A 143 49.732 20.910 122.416 1.00 12.72 A N ATOM 294 NH2 ARG A 143 51.305 19.471 123.287 1.00 14.62 A N ATOM 295 C ARG A 143 50.139 20.214 116.952 1.00 16.25 A C ATOM 296 O ARG A 143 49.478 21.162 116.535 1.00 18.41 A O ATOM 297 N ALA A 144 51.453 20.140 116.787 1.00 14.76 A N ATOM 298 CA ALA A 144 52.165 21.199 116.079 1.00 14.81 A C ATOM 299 CB ALA A 144 53.687 21.021 116.247 1.00 9.68 A C ATOM 300 C ALA A 144 51.763 21.169 114.592 1.00 15.68 A C ATOM 301 O ALA A 144 51.588 22.214 113.970 1.00 14.69 A O ATOM 302 N PHE A 145 51.605 19.968 114.033 1.00 16.80 A N ATOM 303 CA PHE A 145 51.193 19.815 112.632 1.00 17.22 A C ATOM 304 CB PHE A 145 51.386 18.367 112.154 1.00 14.07 A C ATOM 305 CG PHE A 145 52.791 18.045 111.744 1.00 9.59 A C ATOM 306 CD1 PHE A 145 53.433 18.797 110.767 1.00 10.98 A C ATOM 307 CD2 PHE A 145 53.472 16.990 112.326 1.00 9.63 A C ATOM 308 CE1 PHE A 145 54.739 18.503 110.373 1.00 10.38 A C ATOM 309 CE2 PHE A 145 54.781 16.687 111.939 1.00 11.84 A C ATOM 310 CZ PHE A 145 55.414 17.448 110.958 1.00 9.71 A C ATOM 311 C PHE A 145 49.729 20.209 112.438 1.00 19.32 A C ATOM 312 O PHE A 145 49.366 20.790 111.414 1.00 20.25 A O ATOM 313 N ALA A 146 48.889 19.891 113.420 1.00 18.99 A N ATOM 314 CA ALA A 146 47.471 20.224 113.330 1.00 20.15 A C ATOM 315 CB ALA A 146 46.730 19.695 114.542 1.00 16.75 A C ATOM 316 C ALA A 146 47.246 21.727 113.195 1.00 21.23 A C ATOM 317 O ALA A 146 46.272 22.153 112.592 1.00 24.43 A O ATOM 318 N LEU A 147 48.137 22.533 113.764 1.00 23.09 A N ATOM 319 CA LEU A 147 47.996 23.983 113.668 1.00 21.92 A C ATOM 320 CB LEU A 147 49.155 24.698 114.367 1.00 20.86 A C ATOM 321 CG LEU A 147 49.260 24.748 115.894 1.00 24.92 A C ATOM 322 CD1 LEU A 147 50.469 25.598 116.255 1.00 22.84 A C ATOM 323 CD2 LEU A 147 48.001 25.342 116.513 1.00 22.59 A C ATOM 324 C LEU A 147 47.984 24.422 112.206 1.00 22.21 A C ATOM 325 O LEU A 147 47.188 25.265 111.797 1.00 22.01 A O ATOM 326 N TRP A 148 48.884 23.842 111.425 1.00 21.86 A N ATOM 327 CA TRP A 148 49.013 24.196 110.026 1.00 23.11 A C ATOM 328 CB TRP A 148 50.413 23.831 109.534 1.00 19.89 A C ATOM 329 CG TRP A 148 51.513 24.569 110.249 1.00 21.33 A C ATOM 330 CD2 TRP A 148 51.827 25.964 110.138 1.00 21.93 A C ATOM 331 CR2 TRP A 148 52.965 26.203 110.942 1.00 20.27 A C ATOM 332 CR3 TRP A 148 51.259 27.036 109.435 1.00 18.40 A C ATOM 333 CD1 TRP A 148 52.445 24.037 111.100 1.00 20.02 A C ATOM 334 NE1 TRP A 148 53.320 25.012 111.517 1.00 17.63 A N ATOM 335 CZ2 TRP A 148 53.548 27.472 111.059 1.00 19.95 A C ATOM 336 CZ3 TRP A 148 51.838 28.297 109.553 1.00 19.74 A C ATOM 337 CH2 TRP A 148 52.972 28.503 110.359 1.00 18.39 A C ATOM 338 C TRP A 148 47.955 23.571 109.126 1.00 23.44 A C ATOM 339 O TRP A 148 47.419 24.237 108.244 1.00 21.73 A O ATOM 340 N SER A 149 47.645 22.300 109.351 1.00 25.55 A N ATOM 341 CA SER A 149 46.648 21.630 108.531 1.00 27.95 A C ATOM 342 CB SER A 149 46.618 20.127 108.823 1.00 28.12 A C ATOM 343 OG SER A 149 46.132 19.877 110.124 1.00 27.95 A O ATOM 344 C SER A 149 45.274 22.220 108.782 1.00 28.65 A C ATOM 345 O SER A 149 44.340 21.959 108.031 1.00 30.51 A O ATOM 346 N ALA A 150 45.148 23.022 109.833 1.00 27.46 A N ATOM 347 CA ALA A 150 43.864 23.627 110.151 1.00 27.51 A C ATOM 348 CB ALA A 150 43.817 24.013 111.620 1.00 24.47 A C ATOM 349 C ALA A 150 43.552 24.843 109.280 1.00 28.60 A C ATOM 350 O ALA A 150 42.393 25.187 109.091 1.00 28.82 A O ATOM 351 N VAL A 151 44.579 25.492 108.745 1.00 30.95. A N ATOM 352 CA VAL A 151 44.366 26.670 107.909 1.00 30.77 A C ATOM 353 CB VAL A 151 45.144 27.891 108.456 1.00 30.72 A C ATOM 354 OG1 VAL A 151 44.557 28.320 109.784 1.00 32.55 A C ATOM 355 CG2 VAL A 151 46.617 27.546 108.623 1.00 27.92 A C ATOM 356 C VAL A 151 44.765 26.451 106.455 1.00 30.85 A C ATOM 357 O VAL A 151 44.898 27.405 105.691 1.00 31.86 A O ATOM 358 N THR A 152 44.958 25.195 106.072 1.00 30.06 A N ATOM 359 CA THR A 152 45.339 24.879 104.703 1.00 30.51 A C ATOM 360 CB THR A 152 46.879 24.805 104.536 1.00 29.92 A C ATOM 361 OG1 THR A 152 47.390 23.686 105.273 1.00 28.72 A O ATOM 362 CG2 THR A 152 47.538 26.087 105.021 1.00 30.53 A C ATOM 363 C THR A 152 44.760 23.530 104.301 1.00 30.44 A C ATOM 364 O THR A 152 44.171 22.831 105.125 1.00 29.70 A O ATOM 365 N PRO A 153 44.904 23.157 103.017 1.00 30.47 A N ATOM 366 CD PRO A 153 45.298 24.023 101.887 1.00 30.45 A C ATOM 367 CA PRO A 153 44.392 21.875 102.527 1.00 30.14 A C ATOM 368 CB PRO A 153 44.174 22.145 101.042 1.00 30.77 A C ATOM 369 CG PRO A 153 45.304 23.059 100.717 1.00 32.01 A C ATOM 370 C PRO A 153 45.400 20.750 102.768 1.00 29.51. A C ATOM 371 O PRO A 153 45.190 19.619 102.336 1.00 30.25 A O ATOM 372 N LEU A 154 46.496 21.075 103.451 1.00 27.86 A N ATOM 373 CA LEU A 154 47.539 20.100 103.753 1.00 26.19 A C ATOM 374 CB LEU A 154 48.808 20.805 104.233 1.00 26.31 A C ATOM 375 CG LEU A 154 49.491 21.847 103.342 1.00 25.08 A C ATOM 376 CD1 LEU A 154 50.606 22.524 104.124 1.00 23.11 A C ATOM 377 CD2 LEU A 154 50.043 21.196 102.097 1.00 26.17 A C ATOM 378 C LEU A 154 47.104 19.116 104.832 1.00 25.56 A C ATOM 379 O LEU A 154 46.290 19.440 105.693 1.00 26.20 A O ATOM 380 N THR A 155 47.646 17.908 104.764 1.00 24.90 A N ATOM 381 CA THR A 155 47.363 16.875 105.752 1.00 26.31 A C ATOM 382 CB THR A 155 46.481 15.746 105.190 1.00 27.72 A C ATOM 383 OD1 THR A 155 47.094 15.203 104.014 1.00 32.34 A O ATOM 384 CG2 THR A 155 45.088 16.267 104.862 1.00 27.86 A C ATOM 385 C THR A 155 48.711 16.294 106.134 1.00 25.34 A C ATOM 386 O THR A 155 49.670 16.379 105.360 1.00 23.30 A O ATOM 387 N PHE A 156 48.790 15.707 107.323 1.00 23.87 A N ATOM 388 CA PHE A 156 50.044 15.139 107.787 1.00 22.82 A C ATOM 389 CB PHE A 156 50.630 16.046 108.870 1.00 19.73 A C ATOM 390 CG PHE A 156 50.935 17.434 108.375 1.00 15.72 A C ATOM 391 CD1 PHE A 156 52.108 17.693 107.676 1.00 15.50 A C ATOM 392 CD2 PHE A 156 50.011 18.461 108.536 1.00 16.19 A C ATOM 393 CB1 PHE A 156 52.357 18.952 107.139 1.00 14.40 A C ATOM 394 CE2 PHE A 156 50.249 19.725 108.004 1.00 15.79 A C ATOM 395 CZ PHE A 156 51.423 19.972 107.304 1.00 15.01 A C ATOM 396 C PHE A 156 49.864 13.718 108.286 1.00 24.14 A C ATOM 397 O PHE A 156 49.026 13.441 109.145 1.00 26.34 A O ATOM 398 N THR A 157 50.660 12.819 107.726 1.00 24.42 A N ATOM 399 CA THR A 157 50.595 11.410 108.070 1.00 23.69 A C ATOM 400 CB THR A 157 50.245 10.569 106.822 1.00 23.41 A C ATOM 401 OG1 THR A 157 48.935 10.931 106.373 1.00 25.91 A O ATOM 402 CG2 THR A 157 50.277 9.081 107.135 1.00 21.00 A C ATOM 403 C THR A 157 51.915 10.939 108.638 1.00 22.11 A C ATOM 404 O THR A 157 52.984 11.228 108.090 1.00 21.92 A O ATOM 405 N ARG A 158 51.830 10.214 109.745 1.00 22.59 A N ATOM 406 CA ARG A 158 53.015 9.679 110.394 1.00 22.35 A C ATOM 407 CB ARG A 158 52.780 9.534 111.899 1.00 21.18 A C ATOM 408 CG ARG A 158 53.998 9.010 112.630 1.00 21.22 A C ATOM 409 CD ARG A 158 53.758 8.843 114.113 1.00 20.30 A C ATOM 410 NE ARG A 158 54.959 8.340 114.776 1.00 20.99 A N ATOM 411 CZ ARG A 158 55.013 7.974 116.051 1.00 20.64 A C ATOM 412 NH1 ARG A 158 53.931 8.058 116.811 1.00 19.84 A N ATOM 413 NH2 ARG A 158 56.147 7.506 116.560 1.00 20.74 A N ATOM 414 C ARG A 158 53.362 8.320 109.802 1.00 21.92 A C ATOM 415 O ARG A 158 52.508 7.442 109.710 1.00 21.61 A O ATOM 416 N VAL A 159 54.618 8.156 109.399 1.00 24.22 A N ATOM 417 CA VAL A 159 55.092 6.901 108.823 1.00 25.52 A C ATOM 418 CB VAL A 159 55.403 7.059 107.311 1.00 23.23 A C ATOM 419 CG1 VAL A 159 54.147 7.523 106.573 1.00 19.77 A C ATOM 420 CG2 VAL A 159 56.539 8.045 107.109 1.00 21.91 A C ATOM 421 C VAL A 159 56.344 6.469 109.579 1.00 28.57 A C ATOM 422 O VAL A 159 56.842 7.212 110.424 1.00 29.72 A O ATOM 423 N TYR A 160 56.859 5.278 109.282 1.00 31.79 A N ATOM 424 CA TYR A 160 58.033 4.791 109.995 1.00 33.61 A C ATOM 425 CB TYR A 160 57.634 3.596 110.863 1.00 29.27 A C ATOM 426 CG TYR A 160 56.570 3.952 111.873 1.00 28.93 A C ATOM 427 CD1 TYR A 160 55.230 4.056 111.498 1.00 28.23 A C ATOM 428 CE1 TYR A 160 54.256 4.465 112.410 1.00 29.32 A C ATOM 429 CD2 TYR A 160 56.912 4.261 113.191 1.00 28.64 A C ATOM 430 CE2 TYR A 160 55.949 4.670 114.108 1.00 29.60 A C ATOM 431 CZ TYR A 160 54.626 4.772 113.712 1.00 30.04 A C ATOM 432 OH TYR A 160 53.680 5.193 114.616 1.00 32.56 A O ATOM 433 C TYR A 160 59.270 4.449 109.170 1.00 36.31 A C ATOM 434 O TYR A 160 60.097 3.640 109.591 1.00 39.18 A O ATOM 435 N SER A 161 59.414 5.075 108.010 1.00 37.86 A N ATOM 436 CA SER A 161 60.574 4.816 107.174 1.00 39.80 A C ATOM 437 CB SER A 161 60.166 4.018 105.933 1.00 38.63 A C ATOM 438 OG SER A 161 59.238 4.737 105.143 1.00 39.02 A O ATOM 439 C SER A 161 61.231 6.128 106.766 1.00 41.58 A C ATOM 440 O SER A 161 60.664 7.200 106.972 1.00 41.79 A O ATOM 441 N ARG A 162 62.426 6.033 106.187 1.00 44.11 A N ATOM 442 CA ARG A 162 63.188 7.198 105.739 1.00 46.57 A C ATOM 443 CB ARG A 162 64.613 6.790 105.350 1.00 48.67 A C ATOM 444 CG ARG A 162 65.408 6.045 106.418 1.00 53.36 A C ATOM 445 CD ARG A 162 64.757 4.721 106.797 1.00 57.23 A C ATOM 446 NE ARG A 162 65.661 3.839 107.528 1.00 60.31 A N ATOM 447 CZ ARG A 162 65.274 2.728 108.145 1.00 62.63 A C ATOM 448 NH1 ARG A 162 63.997 2.372 108.120 1.00 63.79 A N ATOM 449 NH2 ARG A 162 66.161 1.965 108.777 1.00 62.58 A N ATOM 450 C ARG A 162 62.537 7.862 104.529 1.00 47.42 A C ATOM 451 O ARG A 162 63.027 8.879 104.040 1.00 48.56 A O ATOM 452 N ASP A 163 61.441 7.282 104.048 1.00 48.01 A N. ATOM 453 CA ASP A 163 60.739 7.804 102.876 1.00 46.94 A C ATOM 454 CB ASP A 163 59.909 6.695 102.227 1.00 52.93 A C ATOM 455 CG ASP A 163 60.766 5.584 101.665 1.00 56.71 A C ATOM 456 OD1 ASP A 163 61.681 5.891 100.871 1.00 59.29 A O ATOM 457 OD2 ASP A 163 60.525 4.409 102.013 1.00 61.03 A O ATOM 458 C ASP A 163 59.838 9.008 103.127 1.00 42.48 A C ATOM 459 O ASP A 163 59.350 9.627 102.181 1.00 43.42 A O ATOM 460 N ALA A 164 59.612 9.337 104.392 1.00 35.33 A N ATOM 461 CA ALA A 164 58.768 10.476 104.738 1.00 28.19 A C ATOM 462 CB ALA A 164 58.656 10.591 106.254 1.00 28.52 A C ATOM 463 C ALA A 164 59.332 11.776 104.159 1.00 24.32 A C ATOM 464 O ALA A 164 60.528 11.868 103.859 1.00 18.94 A O ATOM 465 N ASP A 165 58.468 12.776 103.996 1.00 20.55 A N ATOM 466 CA ASP A 165 58.910 14.070 103.491 1.00 19.96 A C ATOM 467 CB ASP A 165 57.732 14.931 103.033 1.00 20.58 A C ATOM 468 CG ASP A 165 56.953 14.302 101.918 1.00 19.34 A C ATOM 469 OD1 ASP A 165 57.577 13.931 100.907 1.00 22.92 A O ATOM 470 OD2 ASP A 165 55.720 14.185 102.053 1.00 20.26 A O ATOM 471 C ASP A 165 59.619 14.808 104.609 1.00 19.50 A C ATOM 472 O ASP A 165 60.669 15.387 104.403 1.00 20.89 A O ATOM 473 N ILE A 166 59.031 14.798 105.798 1.00 18.88 A N ATOM 474 CA ILE A 166 59.638 15.496 106.923 1.00 18.31 A C ATOM 475 CB ILE A 166 58.612 16.435 107.598 1.00 16.76 A C ATOM 476 CG2 ILE A 166 59.241 17.114 108.817 1.00 15.02 A C ATOM 477 CG1 ILE A 166 58.129 17.477 106.581 1.00 16.47 A C ATOM 478 CD1 ILE A 166 57.004 18.367 107.073 1.00 12.28 A C ATOM 479 C ILE A 166 60.198 14.523 107.950 1.00 18.31 A C ATOM 480 O ILE A 166 59.448 13.831 108.635 1.00 19.42 A O ATOM 481 N VAL A 167 61.522 14.453 108.032 1.00 16.42 A N ATOM 482 CA VAL A 167 62.172 13.577 108.992 1.00 14.89 A C ATOM 483 CB VAL A 167 63.410 12.891 108.391 1.00 16.42 A C ATOM 484 CG1 VAL A 167 64.133 12.076 109.464 1.00 14.30 A C ATOM 485 CG2 VAL A 167 62.984 11.982 107.243 1.00 18.08 A C ATOM 486 C VAL A 167 62.581 14.415 110.200 1.00 17.08 A C ATOM 487 O VAL A 167 63.232 15.456 110.064 1.00 13.46 A O ATOM 488 N ILE A 168 62.183 13.943 111.378 1.00 15.49 A N ATOM 489 CA ILE A 168 62.445 14.624 112.633 1.00 16.01 A C ATOM 490 CB ILE A 168 61.145 14.735 113.448 1.00 13.64 A C ATOM 491 CG2 ILE A 168 61.406 15.473 114.755 1.00 14.98 A C ATOM 492 CG1 ILE A 168 60.077 15.427 112.603 1.00 12.69 A C ATOM 493 CD1 ILE A 168 58.685 15.344 113.170 1.00 10.54 A C ATOM 494 C ILE A 168 63.482 13.906 113.486 1.00 16.29 A C ATOM 495 O ILE A 168 63.442 12.693 113.648 1.00 18.46 A O ATOM 496 N GLN A 169 64.414 14.656 114.045 1.00 19.10 A N ATOM 497 CA GLN A 169 65.407 14.028 114.890 1.00 20.39 A C ATOM 498 CB GLN A 169 66.536 13.443 114.043 1.00 23.58 A C ATOM 499 CG GLN A 169 67.428 14.481 113.409 1.00 28.43 A C ATOM 500 CD GLN A 169 68.723 13.890 112.901 1.00 32.40 A C ATOM 501 OE1 GLN A 169 69.551 13.411 113.678 1.00 36.26 A O ATOM 502 NE2 GLN A 169 68.908 13.917 111.591 1.00 33.78 A N ATOM 503 C GLN A 169 65.998 14.991 115.905 1.00 19.32 A C ATOM 504 O GLN A 169 66.009 16.206 115.694 1.00 17.87 A O ATOM 505 N PHE A 170 66.482 14.423 117.005 1.00 15.27 A N ATOM 506 CA PHE A 170 67.124 15.180 118.062 1.00 16.05 A C ATOM 507 CB PHE A 170 66.613 14.740 119.444 1.00 13.11 A C ATOM 508 CG PHE A 170 65.164 15.056 119.690 1.00 11.58 A C ATOM 509 CD1 PHE A 170 64.157 14.272 119.131 1.00 9.60 A C ATOM 510 CD2 PHE A 170 64.807 16.148 120.475 1.00 11.94 A C ATOM 511 CE1 PHE A 170 62.817 14.572 119.352 1.00 10.10 A C ATOM 512 CE2 PHE A 170 63.466 16.458 120.701 1.00 11.51 A C ATOM 513 CZ PHE A 170 62.471 15.671 120.141 1.00 11.15 A C ATOM 514 C PHE A 170 68.611 14.873 117.953 1.00 17.13 A C ATOM 515 O PHE A 170 68.998 13.728 117.747 1.00 18.15 A O ATOM 516 N GLY A 171 69.450 15.889 118.082 1.00 17.88 A N ATOM 517 CA GLY A 171 70.879 15.655 118.006 1.00 19.53 A C ATOM 518 C GLY A 171 71.642 16.630 118.878 1.00 21.64 A C ATOM 519 O GLY A 171 71.083 17.631 119.324 1.00 22.76 A O ATOM 520 N VAL A 172 72.912 16.332 119.138 1.00 23.09 A N ATOM 521 CA VAL A 172 73.756 17.205 119.950 1.00 25.50 A C ATOM 522 CB VAL A 172 74.109 16.560 121.326 1.00 26.03 A C ATOM 523 CG1 VAL A 172 72.844 16.252 122.083 1.00 26.98 A C ATOM 524 CG2 VAL A 172 74.918 15.292 121.134 1.00 25.99 A C ATOM 525 C VAL A 172 75.038 17.489 119.174 1.00 26.07 A C ATOM 526 O VAL A 172 75.653 16.574 118.615 1.00 24.44 A O ATOM 527 N ALA A 173 75.427 18.760 119.139 1.00 27.68 A N ATOM 528 CA ALA A 173 76.618 19.184 118.411 1.00 28.80 A C ATOM 529 CB ALA A 173 77.868 18.664 119.111 1.00 29.58 A C ATOM 530 C ALA A 173 76.548 18.659 116.974 1.00 29.57 A C ATOM 531 O ALA A 173 75.538 18.843 116.289 1.00 27.64 A O ATOM 532 N GLU A 174 77.619 18.006 116.530 1.00 29.27 A N ATOM 533 CA GLU A 174 77.699 17.437 115.189 1.00 32.29 A C ATOM 534 CB GLU A 174 79.078 16.815 114.972 1.00 41.88 A C ATOM 535 CG GLU A 174 80.209 17.511 115.722 1.00 51.63 A C ATOM 536 CD GLU A 174 80.512 18.892 115.178 1.00 57.77 A C ATOM 537 OE1 GLU A 174 81.379 19.584 115.757 1.00 58.88 A O ATOM 538 OE2 GLU A 174 79.888 19.284 114.167 1.00 62.24 A O ATOM 539 C GLU A 174 76.657 16.340 115.076 1.00 30.20 A C ATOM 540 O GLU A 174 76.668 15.409 115.874 1.00 31.68 A O ATOM 541 N HIS A 175 75.768 16.418 114.092 1.00 27.49 A N ATOM 542 CA HIS A 175 74.748 15.385 113.979 1.00 27.72 A C ATOM 543 CB HIS A 175 73.473 15.827 114.688 1.00 24.97 A C ATOM 544 CG HIS A 175 72.928 17.118 114.175 1.00 20.26 A C ATOM 545 CD2 HIS A 175 72.023 17.379 113.203 1.00 17.16 A C ATOM 546 ND1 HIS A 175 73.354 18.341 114.644 1.00 20.15 A N ATOM 547 CE1 HIS A 175 72.734 19.302 113.982 1.00 18.26 A C ATOM 548 NE2 HIS A 175 71.922 18.744 113.102 1.00 15.77 A N ATOM 549 C HIS A 175 74.392 14.949 112.571 1.00 30.79 A C ATOM 550 O HIS A 175 73.257 14.536 112.317 1.00 32.24 A O ATOM 551 N GLY A 176 75.341 15.042 111.647 1.00 32.67 A N ATOM 552 CA GLY A 176 75.048 14.601 110.297 1.00 34.93 A C ATOM 553 C GLY A 176 75.221 15.634 109.213 1.00 36.14 A C ATOM 554 O GLY A 176 76.066 15.481 108.340 1.00 37.19 A O ATOM 555 N ASP A 177 74.399 16.674 109.240 1.00 37.27 A N ATOM 556 CA ASP A 177 74.512 17.721 108.242 1.00 35.71 A C ATOM 557 CB ASP A 177 73.267 18.600 108.231 1.00 34.06 A C ATOM 558 CG ASP A 177 72.828 19.006 109.617 1.00 32.01 A C ATOM 559 OD1 ASP A 177 73.684 19.394 110.439 1.00 28.22 A O ATOM 560 OD2 ASP A 177 71.613 18.942 109.872 1.00 33.33 A O ATOM 561 C ASP A 177 75.734 18.551 108.587 1.00 36.61 A C ATOM 562 O ASP A 177 76.570 18.132 109.389 1.00 40.71 A O ATOM 563 N GLY A 178 75.845 19.730 107.996 1.00 34.57 A N ATOM 564 CA GLY A 178 77.008 20.546 108.278 1.00 36.70 A C ATOM 565 C GLY A 178 76.753 21.721 109.194 1.00 36.80 A C ATOM 566 O GLY A 178 77.520 22.684 109.184 1.00 37.18 A O ATOM 567 N TYR A 179 75.688 21.649 109.991 1.00 37.02 A N ATOM 568 CA TYR A 179 75.344 22.731 110.908 1.00 34.28 A C ATOM 569 CB TYR A 179 74.078 23.436 110.425 1.00 36.20 A C ATOM 570 CG TYR A 179 74.181 23.932 109.003 1.00 42.47 A C ATOM 571 CD1 TYR A 179 73.949 23.076 107.927 1.00 45.68 A C ATOM 572 CE1 TYR A 179 74.065 23.524 106.609 1.00 46.33 A C ATOM 573 CD2 TYR A 179 74.536 25.253 108.728 1.00 44.79 A C ATOM 574 CE2 TYR A 179 74.658 25.712 107.415 1.00 45.00 A C ATOM 575 CZ TYR A 179 74.420 24.843 106.362 1.00 47.34 A C ATOM 576 OH TYR A 179 74.528 25.293 105.062 1.00 48.94 A O ATOM 577 C TYR A 179 75.153 22.235 112.335 1.00 31.65 A C ATOM 578 O TYR A 179 74.033 22.165 112.838 1.00 29.30 A O ATOM 579 N PRO A 180 76.260 21.895 113.014 1.00 31.79 A N ATOM 580 CD PRO A 180 77.653 22.113 112.589 1.00 30.47 A C ATOM 581 CA PRO A 180 76.212 21.401 114.394 1.00 30.83 A C ATOM 582 CB PRO A 180 77.685 21.194 114.739 1.00 31.29 A C ATOM 583 CG PRO A 180 78.370 22.238 113.916 1.00 31.47 A C ATOM 584 C PRO A 180 75.532 22.381 115.335 1.00 28.21 A C ATOM 585 O PRO A 180 75.505 23.579 115.073 1.00 28.60 A O ATOM 586 N PHE A 181 74.971 21.866 116.422 1.00 25.93 A N ATOM 587 CA PHE A 181 74.306 22.721 117.388 1.00 26.27 A C ATOM 588 CB PHE A 181 73.238 21.937 118.158 1.00 23.67 A C ATOM 589 CG PHE A 181 72.012 21.625 117.346 1.00 21.97 A C ATOM 590 CD1 PHE A 181 71.262 22.649 116.778 1.00 22.39 A C. ATOM 591 CD2 PHE A 181 71.590 20.309 117.165 1.00 21.41 A C ATOM 592 CE1 PHE A 181 70.102 22.369 116.040 1.00 22.23 A C ATOM 593 CE2 PHE A 181 70.432 20.019 116.430 1.00 20.84 A C ATOM 594 CZ PHE A 181 69.688 21.052 115.868 1.00 19.15 A C ATOM 595 C PHE A 181 75.351 23.306 118.335 1.00 28.41 A C ATOM 596 O PHE A 181 76.498 22.863 118.354 1.00 27.60 A O ATOM 597 N ASP A 182 74.943 24.290 119.127 1.00 28.53 A N ATOM 598 CA ASP A 182 75.848 24.979 120.031 1.00 29.79 A C ATOM 599 CB ASP A 182 75.723 26.478 119.769 1.00 28.81 A C ATOM 600 CG ASP A 182 74.284 26.937 119.799 1.00 29.97 A C ATOM 601 OD1 ASP A 182 73.464 26.193 120.358 1.00 30.97 A O ATOM 602 OD2 ASP A 182 73.962 28.025 119.284 1.00 31.92 A O ATOM 603 C ASP A 182 75.677 24.718 121.535 1.00 31.81 A C ATOM 604 O ASP A 182 75.941 25.608 122.346 1.00 34.01 A O ATOM 605 N GLY A 183 75.249 23.520 121.921 1.00 31.93 A N ATOM 606 CA GLY A 183 75.085 23.236 123.341 1.00 31.05 A C ATOM 607 C GLY A 183 73.943 24.014 123.976 1.00 32.23 A C ATOM 608 O GLY A 183 73.094 24.524 123.276 1.00 32.15 A O ATOM 609 N LYS A 184 73.923 24.122 125.299 1.00 32.11 A N ATOM 610 CA LYS A 184 72.851 24.832 126.002 1.00 33.02 A C ATOM 611 CB LYS A 184 73.209 24.984 127.484 1.00 37.17 A C ATOM 612 CG LYS A 184 72.020 25.232 128.396 1.00 41.04 A C ATOM 613 CD LYS A 184 71.101 24.017 128.419 1.00 44.80 A C ATOM 614 CE LYS A 184 69.925 24.219 129.353 1.00 45.32 A C ATOM 615 NZ LYS A 184 70.371 24.435 130.752 1.00 48.28 A N ATOM 616 C LYS A 184 72.539 26.207 125.424 1.00 31.99 A C ATOM 617 O LYS A 184 73.445 26.975 125.118 1.00 34.08 A O ATOM 618 N ASP A 185 71.250 26.504 125.278 1.00 30.60 A N ATOM 619 CA ASP A 185 70.777 27.787 124.756 1.00 29.01 A C ATOM 620 CB ASP A 185 71.068 28.895 125.763 1.00 33.03 A C ATOM 621 CG ASP A 185 70.304 28.712 127.046 1.00 36.57 A C ATOM 622 OD1 ASP A 185 69.058 28.796 127.011 1.00 39.21 A O ATOM 623 OD2 ASP A 185 70.947 28.470 128.090 1.00 40.55 A O ATOM 624 C ASP A 185 71.311 28.198 123.394 1.00 26.92 A C ATOM 625 O ASP A 185 71.999 27.438 122.727 1.00 25.74 A O ATOM 626 N GLY A 186 70.992 29.422 122.990 1.00 24.58 A N ATOM 627 CA GLY A 186 71.431 29.904 121.695 1.00 26.41 A C ATOM 628 C GLY A 186 70.472 29.395 120.637 1.00 26.21 A C ATOM 629 O GLY A 186 69.280 29.693 120.691 1.00 27.15 A O ATOM 630 N LEU A 187 70.987 28.625 119.684 1.00 26.00 A N ATOM 631 CA LEU A 187 70.166 28.058 118.622 1.00 25.00 A C ATOM 632 CB LEU A 187 71.057 27.560 117.483 1.00 25.51 A C ATOM 633 CG LEU A 187 70.323 27.068 116.233 1.00 31.44 A C ATOM 634 CD1 LEU A 187 69.618 28.248 115.564 1.00 27.44 A C ATOM 635 CD2 LEU A 187 71.313 26.409 115.271 1.00 32.87 A C ATOM 636 C LEU A 187 69.394 26.885 119.220 1.00 24.47 A C ATOM 637 O LEU A 187 69.996 25.979 119.775 1.00 23.75 A O ATOM 638 N LEU A 188 68.071 26.881 119.097 1.00 22.38 A N ATOM 639 CA LEU A 188 67.272 25.800 119.673 1.00 20.10 A C ATOM 640 CB LEU A 188 65.930 26.349 120.158 1.00 17.21 A C ATOM 641 CG LEU A 188 65.981 27.580 121.077 1.00 19.72 A C ATOM 642 CD1 LEU A 188 64.565 27.997 121.447 1.00 14.44 A C ATOM 643 CD2 LEU A 188 66.791 27.275 122.329 1.00 16.62 A C ATOM 644 C LEU A 188 67.026 24.638 118.712 1.00 21.08 A C ATOM 645 O LEU A 188 66.907 23.477 119.129 1.00 18.95 A O ATOM 646 N ALA A 189 66.956 24.958 117.426 1.00 19.08 A N ATOM 647 CA ALA A 189 66.703 23.963 116.400 1.00 16.54 A C ATOM 648 CB ALA A 189 65.297 23.398 116.575 1.00 16.25 A C ATOM 649 C ALA A 189 66.824 24.626 115.039 1.00 17.08 A C ATOM 650 O ALA A 189 67.110 25.815 114.943 1.00 16.33 A O ATOM 651 N HIS A 190 66.627 23.842 113.988 1.00 16.66 A N ATOM 652 CA HIS A 190 66.656 24.361 112.636 1.00 18.31 A C ATOM 653 CB HIS A 190 68.099 24.705 112.191 1.00 18.50 A C ATOM 654 CG HIS A 190 69.055 23.550 112.164 1.00 17.26 A C ATOM 655 CD2 HIS A 190 68.920 22.281 111.712 1.00 20.42 A C ATOM 656 ND1 HIS A 190 70.369 23.671 112.567 1.00 18.18 A N ATOM 657 CE1 HIS A 190 71.002 22.531 112.365 1.00 17.27 A C ATOM 658 NB2 HIS A 190 70.145 21.671 111.846 1.00 18.89 A N ATOM 659 C HIS A 190 65.982 23.372 111.699 1.00 18.42 A C ATOM 660 O HIS A 190 65.985 22.168 111.956 1.00 18.06 A O ATOM 661 N ALA A 191 65.367 23.887 110.637 1.00 19.52 A N ATOM 662 CA ALA A 191 64.672 23.049 109.659 1.00 20.18 A C ATOM 663 CB ALA A 191 63.163 23.158 109.853 1.00 17.02 A C ATOM 664 C ALA A 191 65.052 23.460 108.242 1.00 22.20 A C ATOM 665 O ALA A 191 65.547 24.563 108.026 1.00 22.82 A O ATOM 666 N PHE A 192 64.822 22.569 107.279 1.00 24.96 A N ATOM 667 CA PHE A 192 65.156 22.847 105.884 1.00 24.10 A C ATOM 668 CB PHE A 192 66.013 21.724 105.303 1.00 24.41 A C ATOM 669 CG PHE A 192 67.299 21.491 106.042 1.00 25.34 A C ATOM 670 CD1 PHE A 192 67.328 20.696 107.184 1.00 27.98 A C ATOM 671 CD2 PHE A 192 68.483 22.059 105.594 1.00 26.82 A C ATOM 672 CE1 PHE A 192 68.524 20.466 107.870 1.00 27.32 A C ATOM 673 CE2 PHE A 192 69.682 21.839 106.267 1.00 27.38 A C ATOM 674 CZ PHE A 192 69.703 21.039 107.410 1.00 28.50 A C ATOM 675 C PHE A 192 63.906 23.012 105.033 1.00 25.05 A C ATOM 676 O PHE A 192 62.891 22.346 105.270 1.00 24.67 A O ATOM 677 N PRO A 193 63.967 23.908 104.027 1.00 25.22 A N ATOM 678 CD PRO A 193 65.156 24.708 103.684 1.00 25.93 A C ATOM 679 CA PRO A 193 62.861 24.203 103.103 1.00 24.58 A C ATOM 680 CB PRO A 193 63.434 25.292 102.195 1.00 22.65 A C ATOM 681 CG PRO A 193 64.542 25.894 102.997 1.00 26.18 A C ATOM 682 C PRO A 193 62.454 22.970 102.299 1.00 24.59 A C ATOM 683 O PRO A 193 63.231 22.018 102.164 1.00 23.68 A O ATOM 684 N PRO A 194 61.233 22.981 101.745 1.00 23.30 A N ATOM 685 CD PRO A 194 60.243 24.072 101.820 1.00 20.97 A C ATOM 686 CA PRO A 194 60.718 21.861 100.949 1.00 24.06 A C ATOM 687 CB PRO A 194 59.445 22.441 100.334 1.00 22.11 A C ATOM 688 CG PRO A 194 58.968 23.371 101.408 1.00 21.80 A C ATOM 689 C PRO A 194 61.710 21.371 99.891 1.00 23.68 A C ATOM 690 O PRO A 194 62.473 22.147 99.325 1.00 21.32 A O ATOM 691 N GLY A 195 61.688 20.071 99.631 1.00 26.27 A N ATOM 692 CA GLY A 195 62.584 19.500 98.645 1.00 26.15 A C ATOM 693 C GLY A 195 62.908 18.059 98.978 1.00 28.20 A C ATOM 694 O GLY A 195 62.355 17.505 99.926 1.00 29.23 A O ATOM 695 N PRO A 196 63.801 17.420 98.211 1.00 28.08 A N ATOM 696 CD PRO A 196 64.340 17.902 96.926 1.00 26.14 A C ATOM 697 CA PRO A 196 64.188 16.025 98.445 1.00 28.94 A C ATOM 698 CB PRO A 196 64.613 15.563 97.057 1.00 27.73 A C ATOM 699 CG PRO A 196 65.288 16.788 96.526 1.00 26.49 A C ATOM 700 C PRO A 196 65.320 15.876 99.472 1.00 29.39 A C ATOM 701 O PRO A 196 65.972 16.855 99.837 1.00 31.26 A O ATOM 702 N GLY A 197 65.542 14.646 99.930 1.00 28.16 A N ATOM 703 CA GLY A 197 66.605 14.374 100.884 1.00 26.43 A C ATOM 704 C GLY A 197 66.466 15.066 102.223 1.00 25.89 A C ATOM 705 O GLY A 197 65.399 15.077 102.803 1.00 26.43 A O ATOM 706 N ILE A 198 67.548 15.648 102.719 1.00 24.59 A N ATOM 707 CA ILE A 198 67.515 16.336 104.000 1.00 27.36 A C ATOM 708 CB ILE A 198 68.929 16.809 104.385 1.00 29.59 A C ATOM 709 CG2 ILE A 198 69.376 17.929 103.447 1.00 29.40 A C ATOM 710 CG1 ILE A 198 68.946 17.268 105.840 1.00 30.60 A C ATOM 711 CD1 ILE A 198 70.323 17.634 106.334 1.00 33.20 A C ATOM 712 C ILE A 198 66.558 17.537 103.966 1.00 29.10 A C ATOM 713 O ILE A 198 66.139 18.048 105.009 1.00 28.33 A O ATOM 714 N GLN A 199 66.212 17.975 102.760 1.00 27.92 A N ATOM 715 CA GLN A 199 65.304 19.100 102.578 1.00 28.08 A C ATOM 716 CB GLN A 199 65.103 19.366 101.081 1.00 31.22 A C ATOM 717 CG GLN A 199 65.534 20.754 100.637 1.00 40.25 A C ATOM 718 CD GLN A 199 66.996 21.044 100.939 1.00 42.74 A C ATOM 719 OE1 GLN A 199 67.459 22.173 100.787 1.00 45.88 A O ATOM 720 NE2 GLN A 199 67.730 20.022 101.362 1.00 44.96 A N ATOM 721 C GLN A 199 63.967 18.794 103.241 1.00 23.32 A C ATOM 722 O GLN A 199 63.442 17.705 103.097 1.00 20.60 A O ATOM 723 N GLY A 200 63.416 19.759 103.967 1.00 23.07 A N ATOM 724 CA GLY A 200 62.147 19.537 104.637 1.00 19.23 A C ATOM 725 C GLY A 200 62.279 18.891 106.009 1.00 18.68 A C ATOM 726 O GLY A 200 61.283 18.719 106.708 1.00 22.62 A O ATOM 727 N ASP A 201 63.496 18.532 106.405 1.00 17.22 A N ATOM 728 CA ASP A 201 63.712 17.903 107.711 1.00 18.97 A C ATOM 729 CB ASP A 201 64.974 17.038 107.687 1.00 16.29 A C ATOM 730 CG ASP A 201 64.834 15.835 106.774 1.00 18.51 A C ATOM 731 OD1 ASP A 201 63.724 15.612 106.260 1.00 15.25 A O ATOM 732 OD2 ASP A 201 65.824 15.104 106.576 1.00 19.34 A O ATOM 733 C ASP A 201 63.813 18.920 108.844 1.00 19.43 A C ATOM 734 O ASP A 201 64.156 20.076 108.621 1.00 21.36 A O ATOM 735 N ALA A 202 63.513 18.476 110.062 1.00 19.70 A N ATOM 736 CA ALA A 202 63.559 19.341 111.239 1.00 18.01 A C ATOM 737 CB ALA A 202 62.142 19.616 111.729 1.00 17.65 A C ATOM 738 C ALA A 202 64.389 18.706 112.350 1.00 18.31 A C ATOM 739 O ALA A 202 64.107 17.588 112.790 1.00 17.93 A O ATOM 740 N HIS A 203 65.407 19.431 112.805 1.00 17.90 A N ATOM 741 CA HIS A 203 66.304 18.945 113.847 1.00 17.65 A C ATOM 742 CB HIS A 203 67.736 18.938 113.313 1.00 15.54 A C ATOM 743 CG HIS A 203 67.906 18.147 112.053 1.00 16.78 A C ATOM 744 CD2 HIS A 203 67.100 17.239 111.453 1.00 14.93 A C ATOM 745 ND1 HIS A 203 69.025 18.248 111.258 1.00 15.86 A N ATOM 746 CE1 HIS A 203 68.902 17.439 110.221 1.00 16.22 A C ATOM 747 NE2 HIS A 203 67.742 16.816 110.316 1.00 14.71 A N ATOM 748 C HIS A 203 66.241 19.782 115.123 1.00 17.94 A C ATOM 749 O HIS A 203 66.248 21.008 115.063 1.00 17.49 A O ATOM 750 N PHE A 204 66.193 19.115 116.275 1.00 17.60 A N ATOM 751 CA PHE A 204 66.133 19.814 117.559 1.00 17.27 A C ATOM 752 CB PHE A 204 64.884 19.389 118.342 1.00 15.27 A C ATOM 753 CG PHE A 204 63.602 19.576 117.579 1.00 15.59 A C ATOM 754 CD1 PHE A 204 63.234 18.678 116.581 1.00 15.30 A C ATQM 755 CD2 PHE A 204 62.790 20.683 117.816 1.00 15.08 A C ATOM 756 CE1 PHE A 204 62.075 18.882 115.826 1.00 17.01 A C ATOM 757 CE2 PHE A 204 61.636 20.899 117.071 1.00 14.70 A C ATOM 758 CZ PHE A 204 61.275 19.998 116.073 1.00 16.71 A C ATOM 759 C PHE A 204 67.378 19.555 118.402 1.00 17.45 A C ATOM 760 O PHE A 204 67.834 18.414 118.510 1.00 15.59 A O ATOM 761 N ASP A 205 67.928 20.619 118.987 1.00 16.31 A N ATOM 762 CA ASP A 205 69.109 20.503 119.837 1.00 16.90 A C ATOM 763 CB ASP A 205 69.729 21.876 120.082 1.00 17.51 A C ATOM 764 CG ASP A 205 71.037 21.788 120.840 1.00 18.97 A C ATOM 765 OD1 ASP A 205 71.305 20.732 121.441 1.00 18.91 A O ATOM 766 OD2 ASP A 205 71.798 22.767 120.836 1.00 18.05 A O ATOM 767 C ASP A 205 68.730 19.883 121.185 1.00 17.81 A C ATOM 768 O ASP A 205 68.024 20.498 121.988 1.00 18.19 A O ATOM 769 N ASP A 206 69.208 18.670 121.436 1.00 19.02 A N ATOM 770 CA ASP A 206 68.880 17.994 122.676 1.00 20.78 A C ATOM 771 CB ASP A 206 68.881 16.473 122.468 1.00 22.45 A C ATOM 772 CG ASP A 206 68.015 15.737 123.497 1.00 25.21 A C ATOM 773 OD1 ASP A 206 67.013 16.317 123.968 1.00 26.38 A O ATOM 774 OD2 ASP A 206 68.321 14.574 123.822 1.00 24.25 A O ATOM 775 C ASP A 206 69.781 18.386 123.847 1.00 21.59 A C ATOM 776 O ASP A 206 69.827 17.692 124.849 1.00 23.96 A O ATOM 777 N ASP A 207 70.513 19.488 123.715 1.00 23.27 A N ATOM 778 CA ASP A 207 71.331 19.969 124.823 1.00 22.12 A C ATOM 779 CB ASP A 207 72.605 20.664 124.342 1.00 23.08 A C ATOM 780 CG ASP A 207 73.809 19.738 124.348 1.00 24.02 A C ATOM 781 OD1 ASP A 207 73.806 18.762 125.124 1.00 26.09 A O ATOM 782 OD2 ASP A 207 74.766 19.989 123.591 1.00 23.97 A O ATOM 783 C ASP A 207 70.458 20.966 125.570 1.00 21.36 A C ATOM 784 O ASP A 207 70.817 21.459 126.634 1.00 22.22 A O ATOM 785 N GLU A 208 69.303 21.255 124.982 1.00 20.40 A N ATOM 786 CA GLU A 208 68.341 22.172 125.567 1.00 21.00 A C ATOM 787 CB GLU A 208 67.477 22.810 124.475 1.00 22.83 A C ATOM 788 CG GLU A 208 68.262 23.464 123.363 1.00 27.27 A C ATOM 789 CD GLU A 208 68.931 24.732 123.805 1.00 29.69 A C ATOM 790 OE1 GLU A 208 69.277 24.846 124.996 1.00 36.53 A O ATOM 791 OE2 GLU A 208 69.119 25.620 122.959 1.00 34.99 A O ATOM 792 C GLU A 208 67.446 21.345 126.464 1.00 19.62 A C ATOM 793 O GLU A 208 67.323 20.140 126.271 1.00 18.21 A O ATOM 794 N LEU A 209 66.831 21.990 127.447 1.00 18.09 A N ATOM 795 CA LEU A 209 65.898 21.311 128.331 1.00 17.54 A C ATOM 796 CB LEU A 209 65.887 21.982 129.710 1.00 15.57 A C ATOM 797 CG LEU A 209 64.850 21.473 130.714 1.00 19.72 A C ATOM 798 CD1 LEU A 209 65.072 20.004 130.986 1.00 18.15 A C ATOM 799 CD2 LEU A 209 64.947 22.273 132.008 1.00 18.92 A C ATOM 800 C LEU A 209 64.529 21.445 127.653 1.00 16.85 A C ATOM 801 O LEU A 209 64.001 22.549 127.519 1.00 18.96 A O ATOM 802 N TRP A 210 63.974 20.328 127.197 1.00 15.69 A N ATOM 803 CA TRP A 210 62.678 20.347 126.531 1.00 14.68 A C ATOM 804 CB TRP A 210 62.628 19.319 125.384 1.00 12.69 A C ATOM 805 CG TRP A 210 63.520 19.686 124.252 1.00 14.19 A C ATOM 806 CD2 TRP A 210 63.396 20.834 123.402 1.00 14.74 A C ATOM 807 CE2 TRP A 210 64.531 20.855 122.562 1.00 13.82 A C ATOM 808 CE3 TRP A 210 62.438 21.850 123.273 1.00 13.00 A C ATOM 809 CD1 TRP A 210 64.688 19.072 123.893 1.00 15.08 A C ATOM 810 NE1 TRP A 210 65.302 19.770 122.885 1.00 15.30 A N ATOM 811 CZ2 TRP A 210 64.736 21.854 121.605 1.00 12.58 A C ATOM 812 CZ3 TRP A 210 62.646 22.845 122.319 1.00 11.89 A C ATOM 813 CH2 TRP A 210 63.787 22.837 121.499 1.00 10.54 A C ATOM 814 C TRP A 210 61.549 20.080 127.503 1.00 14.10 A C ATOM 815 O TRP A 210 61.614 19.147 128.301 1.00 12.40 A O ATOM 816 N SER A 211 60.504 20.897 127.406 1.00 13.94 A N ATOM 817 CA SER A 211 59.347 20.791 128.272 1.00 13.15 A C ATOM 818 CB SER A 211 59.568 21.682 129.492 1.00 14.15 A C ATOM 819 OG SER A 211 58.635 21.392 130.505 1.00 17.46 A O ATOM 820 C SER A 211 58.102 21.243 127.505 1.00 15.84 A C ATOM 821 O SER A 211 58.080 21.195 126.280 1.00 17.08 A O ATOM 822 N LEU A 212 57.068 21.667 128.233 1.00 15.21 A N ATOM 823 CA LEU A 212 55.819 22.160 127.645 1.00 13.96 A C ATOM 824 CB LEU A 212 54.836 21.018 127.391 1.00 10.99 A C ATOM 825 CG LEU A 212 55.168 19.921 126.378 1.00 11.66 A C ATOM 826 CD1 LEU A 212 54.139 18.817 126.510 1.00 8.67 A C ATOM 827 CD2 LEU A 212 55.202 20.494 124.967 1.00 7.27 A U ATOM 828 C LEU A 212 55.180 23.125 128.635 1.00 17.00 A C ATOM 829 O LEU A 212 55.367 22.992 129.837 1.00 19.75 A O ATOM 830 N GLY A 213 54.421 24.088 128.132 1.00 19.26 A N ATOM 831 CA GLY A 213 53.748 25.037 129.003 1.00 20.32 A C ATOM 832 C GLY A 213 54.639 26.040 129.713 1.00 19.73 A C ATOM 833 O GLY A 213 55.759 26.294 129.285 1.00 20.34 A O ATOM 834 N LYS A 214 54.123 26.618 130.795 1.00 20.81 A N ATOM 835 CA LYS A 214 54.861 27.597 131.588 1.00 21.44 A C ATOM 836 CB LYS A 214 53.909 28.339 132.537 1.00 23.26 A C ATOM 837 CG LYS A 214 52.925 29.266 13 1.838 1.00 25.72 A C ATOM 838 CD LYS A 214 51.935 29.898 132.805 1.00 27.35 A C ATOM 839 CE LYS A 214 51.002 28.859 133.402 1.00 30.75 A C ATOM 840 NZ LYS A 214 49.866 29.485 134.138 1.00 35.19 A N ATOM 841 C LYS A 214 55.917 26.863 132.398 1.00 21.38 A C ATOM 842 O LYS A 214 55.743 25.688 132.729 1.00 22.09 A O ATOM 843 N GLY A 215 57.008 27.548 132.721 1.00 19.58 A N ATOM 844 CA GLY A 215 58.061 26.911 133.491 1.00 20.65 A C ATOM 845 C GLY A 215 59.403 27.007 132.798 1.00 20.80 A C ATOM 846 O GLY A 215 59.496 27.528 131.689 1.00 20.47 A O ATOM 847 N GLN A 391 60.449 26.500 133.439 1.00 21.31 A N ATOM 848 CA GLN A 391 61.779 26.564 132.848 1.00 22.25 A C ATOM 849 CB GLN A 391 62.851 26.279 133.917 1.00 26.72 A C ATOM 850 CG GLN A 391 63.213 24.832 134.110 1.00 34.22 A C ATOM 851 CD GLN A 391 62.000 23.953 134.238 1.00 41.18 A C ATOM 852 OE1 GLN A 391 61.117 24.211 135.054 1.00 48.75 A O ATOM 853 NE2 GLN A 391 61.944 22.903 133.427 1.00 46.74 A N ATOM 854 C GLN A 391 61.886 25.585 131.676 1.00 20.85 A C ATOM 855 O GLN A 391 61.097 24.654 131.561 1.00 20.10 A O ATOM 856 N GLY A 392 62.866 25.794 130.808 1.00 19.12 A N ATOM 857 CA GLY A 392 63.005 24.931 129.653 1.00 20.95 A C ATOM 858 C GLY A 392 62.266 25.565 128.487 1.00 19.62 A C ATOM 859 O GLY A 392 61.669 26.627 128.637 1.00 17.25 A O ATOM 860 N TYR A 393 62.301 24.921 127.328 1.00 19.08 A N ATOM 861 CA TYR A 393 61.637 25.454 126.141 1.00 17.64 A C ATOM 862 CB TYR A 393 62.646 25.560 125.000 1.00 18.65 A C ATOM 863 CG TYR A 393 63.773 26.534 125.256 1.00 18.22 A C ATOM 864 CD1 TYR A 393 63.586 27.905 125.079 1.00 19.12 A C ATOM 865 CE1 TYR A 393 64.626 28.807 125.291 1.00 20.27 A C ATOM 866 CD2 TYR A 393 65.036 26.084 125.660 1.00 18.43 A C ATOM 867 CE2 TYR A 393 66.091 26.980 125.878 1.00 18.43 A C ATOM 868 CZ TYR A 393 65.879 28.339 125.691 1.00 20.99 A C ATOM 869 OH TYR A 393 66.911 29.229 125.892 1.00 18.81 A O ATOM 870 C TYR A 393 60.474 24.563 125.714 1.00 16.46 A C ATOM 871 O TYR A 393 60.552 23.343 125.812 1.00 18.48 A O ATOM 872 N SER A 394 59.393 25.165 125.238 1.00 16.19 A N ATOM 873 CA SER A 394 58.248 24.376 124.799 1.00 16.88 A C ATOM 874 CB SER A 394 57.026 25.268 124.581 1.00 15.95 A C ATOM 875 OG SER A 394 55.900 24.491 124.195 1.00 16.81 A O ATOM 876 C SER A 394 58.555 23.638 123.501 1.00 16.05 A C ATOM 877 O SER A 394 58.781 24.262 122.468 1.00 17.59 A O ATOM 878 N LEU A 395 58.563 22.311 123.557 1.00 13.28 A N ATOM 879 CA LEU A 395 58.825 21.508 122.373 1.00 13.52 A C ATOM 880 CB LEU A 395 58.874 20.022 122.734 1.00 9.81 A C ATOM 881 CG LEU A 395 59.158 19.078 121.559 1.00 10.42 A C ATOM 882 CD1 LEU A 395 60.518 19.417 120.974 1.00 8.66 A C ATOM 883 CD2 LEU A 395 59.117 17.618 122.012 1.00 7.01 A C ATOM 884 C LEU A 395 57.720 21.758 121.345 1.00 13.87 A C ATOM 885 O LEU A 395 57.979 21.792 120.149 1.00 15.88 A O ATOM 886 N PHE A 396 56.495 21.936 121.836 1.00 13.30 A N ATOM 887 CA PHE A 396 55.319 22.195 121.010 1.00 13.78 A C ATOM 888 CB PHE A 396 54.069 22.270 121.907 1.00 14.03 A C ATOM 889 CG PHE A 396 52.850 22.840 121.225 1.00 15.47 A C ATOM 890 CD1 PHE A 396 52.243 22.168 120.167 1.00 16.74 A C ATOM 891 CD2 PHE A 396 52.322 24.064 121.632 1.00 16.39 A C ATOM 892 CE1 PHE A 396 51.128 22.706 119.518 1.00 15.98 A C ATOM 893 CE2 PHE A 396 51.211 24.611 120.993 1.00 17.97 A C ATOM 894 CZ PHE A 396 50.611 23.929 119.929 1.00 16.67 A C ATOM 895 C PHE A 396 55.440 23.476 120.178 1.00 15.62 A C ATOM 896 O PHE A 396 55.242 23.455 118.958 1.00 15.38 A O ATOM 897 N LEU A 397 55.756 24.587 120.837 1.00 14.66 A N ATOM 898 CA LEU A 397 55.892 25.861 120.148 1.00 14.57 A C ATOM 899 CB LEU A 397 55.998 27.009 121.155 1.00 16.23 A C ATOM 900 CG LEU A 397 54.739 27.366 121.951 1.00 19.61 A C ATOM 901 CD1 LEU A 397 55.033 28.532 122.908 1.00 17.04 A C ATOM 902 CD2 LEU A 397 53.615 27.734 120.982 1.00 18.70 A C ATOM 903 C LEU A 397 57.084 25.912 119.202 1.00 16.31 A C ATOM 904 O LEU A 397 57.002 26.511 118.132 1.00 18.67 A O ATOM 905 N VAL A 398 58.198 25.299 119.591 1.00 17.18 A N ATOM 906 CA VAL A 398 59.379 25.309 118.738 1.00 16.87 A C ATOM 907 CB VAL A 398 60.643 24.855 119.513 1.00 15.03 A C ATOM 908 CG1 VAL A 398 61.838 24.750 118.562 1.00 7.55 A C ATOM 909 CG2 VAL A 398 60.953 25.867 120.636 1.00 13.62 A C ATOM 910 C VAL A 398 59.157 24.410 117.524 1.00 17.35 A C ATOM 911 O VAL A 398 59.610 24.715 116.427 1.00 16.12 A O ATOM 912 N ALA A 399 58.446 23.307 117.725 1.00 17.18 A N ATOM 913 CA ALA A 399 58.159 22.386 116.629 1.00 18.10 A C ATOM 914 CB ALA A 399 57.440 21.146 117.155 1.00 17.14 A C ATOM 915 C ALA A 399 57.296 23.084 115.583 1.00 16.31 A C ATOM 916 O ALA A 399 57.540 22.962 114.387 1.00 17.90 A O ATOM 917 N ALA A 400 56.288 23.814 116.048 1.00 16.32 A N ATOM 918 CA ALA A 400 55.385 24.531 115.161 1.00 16.53 A C ATOM 919 CB ALA A 400 54.340 25.283 115.970 1.00 11.88 A C ATOM 920 C ALA A 400 56.162 25.495 114.278 1.00 17.89 A C ATOM 921 O ALA A 400 55.859 25.640 113.101 1.00 18.21 A O ATOM 922 N HIS A 401 57.169 26.142 114.858 1.00 18.94 A N ATOM 923 CA HIS A 401 58.009 27.094 114.140 1.00 16.00 A C ATOM 924 CB HIS A 401 58.934 27.812 115.123 1.00 15.08 A C ATOM 925 CG HIS A 401 59.800 28.858 114.490 1.00 16.72 A C ATOM 926 CD2 HIS A 401 61.049 28.788 113.972 1.00 11.82 A C ATOM 927 ND1 HIS A 401 59.400 30.169 114.344 1.00 16.08 A N ATOM 928 CE1 HIS A 401 60.367 30.860 113.767 1.00 16.27 A C ATOM 929 NE2 HIS A 401 61.377 30.045 113.531 1.00 10.47 A N ATOM 930 C HIS A 401 58.849 26.371 113.091 1.00 17.48 A C ATOM 931 O HIS A 401 58.899 26.785 111.939 1.00 17.04 A O ATOM 932 N GLU A 402 59.512 25.292 113.497 1.00 16.98 A N ATOM 933 CA GLU A 402 60.346 24.523 112.583 1.00 19.94 A C ATOM 934 CB GLU A 402 61.058 23.374 113.311 1.00 20.34 A C ATOM 935 CG GLU A 402 62.029 23.804 114.410 1.00 20.68 A C ATOM 936 CD GLU A 402 62.758 25.100 114.095 1.00 17.45 A C ATOM 937 OE1 GLU A 402 63.300 25.234 112.987 1.00 18.70 A O ATOM 938 OE2 GLU A 402 62.793 25.984 114.967 1.00 17.38 A O ATOM 939 C GLU A 402 59.522 23.952 111.432 1.00 20.70 A C ATOM 940 O GLU A 402 59.961 23.972 110.285 1.00 20.70 A O ATOM 941 N PHE A 403 58.336 23.437 111.735 1.00 20.02 A N ATOM 942 CA PHE A 403 57.482 22.889 110.691 1.00 20.64 A C ATOM 943 CB PHE A 403 56.262 22.184 111.293 1.00 20.51 A C ATOM 944 CG PHE A 403 56.608 21.005 112.173 1.00 20.43 A C ATOM 945 CD1 PHE A 403 57.865 20.398 112.094 1.00 17.64 A C ATOM 946 CD2 PHE A 403 55.678 20.509 113.087 1.00 14.31 A C ATOM 947 CE1 PHE A 403 58.192 19.319 112.916 1.00 18.71 A C ATOM 948 CE2 PHE A 403 55.988 19.424 113.918 1.00 12.75 A C ATOM 949 CZ PHE A 403 57.243 18.826 113.838 1.00 15.90 A C ATOM 950 C PHE A 403 57.040 23.998 109.732 1.00 20.93 A C ATOM 951 O PHE A 403 56.699 23.728 108.587 1.00 20.08 A O ATOM 952 N GLY A 404 57.041 25.241 110.208 1.00 20.24 A N ATOM 953 CA GLY A 404 56.685 26.355 109.352 1.00 18.45 A C ATOM 954 C GLY A 404 57.748 26.442 108.263 1.00 19.06 A C ATOM 955 O GLY A 404 57.438 26.584 107.082 1.00 18.85 A O ATOM 956 N HIS A 405 59.011 26.353 108.666 1.00 17.32 A N ATOM 957 CA HIS A 405 60.119 26.382 107.718 1.00 18.09 A C ATOM 958 CB HIS A 405 61.460 26.317 108.446 1.00 15.13 A C ATOM 959 CG HIS A 405 61.859 27.600 109.095 1.00 19.30 A C ATOM 960 CD2 HIS A 405 62.362 27.859 110.323 1.00 15.40 A C ATOM 961 ND1 HIS A 405 61.769 28.816 108.452 1.00 18.08 A N ATOM 962 CE1 HIS A 405 62.197 29.769 109.258 1.00 17.34 A C ATOM 963 NE2 HIS A 405 62.563 29.214 110.399 1.00 18.40 A N ATOM 964 C HIS A 405 60.040 25.195 106.761 1.00 18.79 A C ATOM 965 O HIS A 405 60.171 25.352 105.554 1.00 22.20 A O ATOM 966 N ALA A 406 59.838 24.007 107.320 1.00 18.37 A N ATOM 967 CA ALA A 406 59.754 22.780 106.545 1.00 17.99 A C ATOM 968 CB ALA A 406 59.511 21.606 107.484 1.00 15.77 A C ATOM 969 C ALA A 406 58.665 22.838 105.468 1.00 17.88 A C ATOM 970 O ALA A 406 58.673 22.045 104.535 1.00 15.94 A O ATOM 971 N LEU A 407 57.730 23.173 105.612 1.00 20.32 A N ATOM 972 CA LEU A 407 56.646 23.935 104.647 1.00 22.45 A C ATOM 973 CB LEU A 407 55.307 24.158 105.367 1.00 21.52 A C ATOM 974 CG LEU A 407 54.789 23.030 106.266 1.00 22.77 A C ATOM 975 CD1 LEU A 407 53.461 23.421 106.888 1.00 19.54 A C ATOM 976 CD2 LEU A 407 54.629 21.766 105.447 1.00 25.90 A C ATOM 977 C LEU A 407 56.921 25.103 103.694 1.00 23.47 A C ATOM 978 O LEU A 407 56.093 25.422 102.844 1.00 23.57 A O ATOM 979 N GLY A 408 58.077 25.743 103.852 1.00 22.90 A N ATOM 980 CA GLY A 408 58.444 26.847 102.983 1.00 23.36 A C ATOM 981 C GLY A 408 58.411 28.268 103.528 1.00 24.25 A C ATOM 982 O GLY A 408 58.891 29.190 102.868 1.00 22.84 A O ATOM 983 N LEU A 409 57.855 28.463 104.719 1.00 25.11 A N ATOM 984 CA LEU A 409 57.777 29.804 105.290 1.00 24.70 A C ATOM 985 CB LEU A 409 56.853 29.828 106.508 1.00 22.64 A C ATOM 986 CG LEU A 409 55.352 29.682 106.281 1.00 25.21 A C ATOM 987 CD1 LEU A 409 54.639 29.943 107.588 1.00 21.69 A C ATOM 988 CD2 LEU A 409 54.880 30.664 105.212 1.00 24.00 A C ATOM 989 C LEU A 409 59.123 30.347 105.711 1.00 25.87 A C ATOM 990 O LEU A 409 59.989 29.598 106.156 1.00 26.76 A O ATOM 991 N ASP A 410 59.294 31.656 105.558 1.00 27.29 A N ATOM 992 CA ASP A 410 60.517 32.323 105.980 1.00 29.12 A C ATOM 993 CB ASP A 410 60.990 33.338 104.933 1.00 34.79 A C ATOM 994 CG ASP A 410 61.553 32.678 103.687 1.00 42.97 A C ATOM 995 OD1 ASP A 410 62.184 31.602 103.799 1.00 48.11 A O ATOM 996 OD2 ASP A 410 61.381 33.247 102.590 1.00 47.38 A O ATOM 997 C ASP A 410 60.188 33.050 107.289 1.00 27.33 A C ATOM 998 O ASP A 410 59.046 33.026 107.751 1.00 19.85 A O ATOM 999 N HIS A 411 61.190 33.687 107.883 1.00 25.92 A N ATOM 1000 CA HIS A 411 60.995 34.418 109.128 1.00 27.93 A C ATOM 1001 CB HIS A 411 62.345 34.843 109.699 1.00 25.18 A C ATOM 1002 CG HIS A 411 63.056 33.747 110.430 1.00 25.67 A C ATOM 1003 CD2 HIS A 411 62.579 32.692 111.134 1.00 22.64 A C ATOM 1004 ND1 HIS A 411 64.429 33.660 110.493 1.00 24.52 A N ATOM 1005 CE1 HIS A 411 64.768 32.596 111.199 1.00 24.55 A C ATOM 1006 NE2 HIS A 411 63.664 31.992 111.598 1.00 21.02 A N ATOM 1007 C HIS A 411 60.103 35.634 108.947 1.00 28.39 A C ATOM 1008 O HIS A 411 60.096 36.257 107.890 1.00 27.54 A O ATOM 1009 N SER A 412 59.348 35.953 109.992 1.00 28.70 A N ATOM 1010 CA SER A 412 58.441 37.090 109.989 1.00 28.94 A C ATOM 1011 CE SER A 412 57.139 36.716 110.696 1.00 27.79 A C ATOM 1012 OG SER A 412 56.288 37.836 110.831 1.00 28.82 A O ATOM 1013 C SER A 412 59.090 38.264 110.708 1.00 30.69 A C ATOM 1014 O SER A 412 60.020 38.081 111.489 1.00 31.96 A O ATOM 1015 N SER A 413 58.601 39.468 110.437 1.00 30.98 A N ATOM 1016 CA SER A 413 59.132 40.664 111.075 1.00 33.39 A C ATOM 1017 CB SER A 413 59.334 41.775 110.039 1.00 34.31 A C ATOM 1018 OG SER A 413 58.154 42.003 109.294 1.00 35.39 A O ATOM 1019 C SER A 413 58.175 41.125 112.166 1.00 32.91 A C ATOM 1020 O SER A 413 58.454 42.076 112.893 1.00 35.58 A O ATOM 1021 N VAL A 414 57.043 40.436 112.264 1.00 31.58 A N ATOM 1022 CA VAL A 414 56.023 40.725 113.264 1.00 31.56 A C ATOM 1023 CB VAL A 414 54.637 40.234 112.792 1.00 31.76 A C ATOM 1024 CG1 VAL A 414 53.578 40.582 113.816 1.00 31.52 A C ATOM 1025 CG2 VAL A 414 54.304 40.849 111.455 1.00 30.36 A C ATOM 1026 C VAL A 414 56.399 40.007 114.564 1.00 31.65 A C ATOM 1027 O VAL A 414 56.415 38.778 114.630 1.00 30.34 A O ATOM 1028 N PRO A 415 56.696 40.775 115.620 1.00 31.44 A N ATOM 1029 CD PRO A 415 56.730 42.248 115.656 1.00 29.01 A C ATOM 1030 CA PRO A 415 57.080 40.220 116.920 1.00 28.81 A C ATOM 1031 CB PRO A 415 57.176 41.461 117.802 1.00 29.09 A C ATOM 1032 CG PRO A 415 57.628 42.513 116.837 1.00 27.34 A C ATOM 1033 C PRO A 415 56.156 39.157 117.503 1.00 26.99 A C ATOM 1034 O PRO A 415 56.626 38.199 118.098 1.00 26.82 A O ATOM 1035 N GLU A 416 54.849 39.316 117.336 1.00 28.55 A N ATOM 1036 CA GLU A 416 53.907 38.343 117.881 1.00 29.16 A C ATOM 1037 CB GLU A 416 52.597 39.029 118.276 1.00 33.01 A C ATOM 1038 CG GLU A 416 52.180 40.147 117.341 1.00 42.66 A C ATOM 1039 CD GLU A 416 52.947 41.437 117.590 1.00 43.72 A C ATOM 1040 OE1 GLU A 416 53.148 42.204 116.626 1.00 43.99 A O ATOM 1041 OE2 GLU A 416 53.336 41.690 118.752 1.00 46.02 A O ATOM 1042 C GLU A 416 53.612 37.163 116.957 1.00 28.85 A C ATOM 1043 O GLU A 416 52.820 36.289 117.297 1.00 30.41 A O ATOM 1044 N ALA A 417 54.257 37.125 115.798 1.00 26.45 A N ATOM 1045 CA ALA A 417 54.037 36.029 114.867 1.00 24.95 A C ATOM 1046 CB ALA A 417 54.429 36.452 113.456 1.00 23.05 A C ATOM 1047 C ALA A 417 54.868 34.826 115.303 1.00 24.52 A C ATOM 1048 O ALA A 417 55.952 34.986 115.861 1.00 23.59 A O ATOM 1049 N LEU A 418 54.354 33.625 115.049 1.00 22.60 A N ATOM 1050 CA LEU A 418 55.060 32.399 115.396 1.00 21.25 A C ATOM 1051 CB LEU A 418 54.186 31.183 115.084 1.00 24.09 A C ATOM 1052 CG LEU A 418 54.819 29.794 115.255 1.00 25.61 A C ATOM 1053 CD1 LEU A 418 55.205 29.584 116.704 1.00 24.01 A C ATOM 1054 CD2 LEU A 418 53.851 28.711 114.802 1.00 24.22 A C ATOM 1055 C LEU A 418 56.378 32.281 114.639 1.00 20.33 A C ATOM 1056 O LEU A 418 57.336 31.699 115.139 1.00 17.86 A O ATOM 1057 N MET A 419 56.425 32.836 113.431 1.00 20.15 A N ATOM 1058 CA MET A 419 57.632 32.763 112.620 1.00 20.11 A C ATOM 1059 CB MET A 419 57.286 32.817 111.130 1.00 19.41 A C ATOM 1060 CG MET A 419 56.562 31.575 110.616 1.00 18.20 A C ATOM 1061 SD MET A 419 57.267 29.973 111.160 1.00 18.41 A S ATOM 1062 CE MET A 419 58.852 29.969 110.370 1.00 13.77 A C ATOM 1063 C MET A 419 58.678 33.816 112.953 1.00 20.18 A C ATOM 1064 O MET A 419 59.679 33.946 112.256 1.00 20.02 A O ATOM 1065 N TYR A 420 58.450 34.571 114.022 1.00 22.13 A N ATOM 1066 CA TYR A 420 59.433 35.561 114.443 1.00 23.96 A C ATOM 1067 CB TYR A 420 58.921 36.336 115.653 1.00 28.74 A C ATOM 1068 CG TYR A 420 59.721 37.578 115.957 1.00 33.66 A C ATOM 1069 CD1 TYR A 420 59.747 38.654 115.064 1.00 35.38 A C ATOM 1070 CE1 TYR A 420 60.495 39.791 115.334 1.00 36.85 A C ATOM 1071 CD2 TYR A 420 60.464 37.674 117.128 1.00 35.51 A C ATOM 1072 CE2 TYR A 420 61.215 38.804 117.409 1.00 38.35 A C ATOM 1073 CZ TYR A 420 61.228 39.858 116.512 1.00 40.13 A C ATOM 1074 OH TYR A 420 61.973 40.976 116.801 1.00 41.02 A O ATOM 1075 C TYR A 420 60.679 34.746 114.812 1.00 22.16 A C ATOM 1076 O TYR A 420 60.583 33.744 115.515 1.00 20.07 A O ATOM 1077 N PRO A 421 61.863 35.172 114.347 1.00 23.33 A N ATOM 1078 CD PRO A 421 62.072 36.447 113.634 1.00 24.71 A C ATOM 1079 CA PRO A 421 63.148 34.501 114.591 1.00 24.11 A C ATOM 1080 CB PRO A 421 64.129 35.342 113.773 1.00 24.83 A C ATOM 1081 CG PRO A 421 63.542 36.703 113.850 1.00 23.46 A C ATOM 1082 C PRO A 421 63.624 34.301 116.028 1.00 24.67 A C ATOM 1083 O PRO A 421 64.649 33.659 116.258 1.00 23.19 A O ATOM 1084 N MET A 422 62.870 34.827 116.986 1.00 23.77 A N ATOM 1085 CA MET A 422 63.228 34.732 118.393 1.00 24.04 A C ATOM 1086 CB MET A 422 63.351 36.148 118.961 1.00 29.95 A C ATOM 1087 CG MET A 422 63.671 36.231 120.433 1.00 39.49 A C ATOM 1088 SD MET A 422 63.479 37.927 121.034 1.00 49.06 A S ATOM 1089 CE MET A 422 61.893 37.842 121.866 1.00 39.08 A C ATOM 1090 C MET A 422 62.181 33.938 119.171 1.00 22.85 A C ATOM 1091 O MET A 422 60.983 34.062 118.915 1.00 21.77 A O ATOM 1092 N TYR A 423 62.626 33.117 120.114 1.00 19.77 A N ATOM 1093 CA TYR A 423 61.699 32.324 120.913 1.00 21.78 A C ATOM 1094 CB TYR A 423 62.441 31.214 121.659 1.00 19.09 A C ATOM 1095 CG TYR A 423 61.551 30.425 122.599 1.00 18.13 A C ATOM 1096 CD1 TYR A 423 60.797 29.344 122.139 1.00 18.66 A C ATOM 1097 CE1 TYR A 423 59.962 28.623 122.996 1.00 16.35 A C ATOM 1098 CD2 TYR A 423 61.445 30.769 123.946 1.00 17.67 A C ATOM 1099 CE2 TYR A 423 60.612 30.059 124.811 1.00 17.18 A C ATOM 1100 CZ TYR A 423 59.874 28.987 124.330 1.00 19.92 A C ATOM 1101 OH TYR A 423 59.053 28.278 125.182 1.00 18.58 A O ATOM 1102 C TYR A 423 60.964 33.168 121.950 1.00 23.28 A C ATOM 1103 O TYR A 423 61.568 34.001 122.616 1.00 23.95 A O ATOM 1104 N ARG A 424 59.662 32.942 122.087 1.00 25.46 A N ATOM 1105 CA ARG A 424 58.869 33.651 123.084 1.00 31.01 A C ATOM 1106 CB ARG A 424 58.376 35.005 122.550 1.00 35.79 A C ATOM 1107 CG ARG A 424 57.230 34.932 121.573 1.00 43.60 A C ATOM 1108 CD ARG A 424 56.693 36.313 121.235 1.00 50.63 A C ATOM 1109 NE ARG A 424 55.481 36.228 120.420 1.00 58.11 A N ATOM 1110 CZ ARG A 424 54.340 35.676 120.828 1.00 62.35 A C ATOM 1111 NH1 ARG A 424 54.247 35.158 122.049 1.00 65.08 A N ATOM 1112 NH2 ARG A 424 53.291 35.634 120.015 1.00 62.97 A N ATOM 1113 C ARG A 424 57.690 32.777 123.499 1.00 29.80 A C ATOM 1114 O ARG A 424 56.830 32.450 122.691 1.00 29.90 A O ATOM 1115 N PHE A 425 57.654 32.374 124.762 1.00 29.63 A N ATOM 1116 CA PHE A 425 56.555 31.534 125.203 1.00 28.26 A C ATOM 1117 CB PHE A 425 56.807 30.963 126.596 1.00 24.65 A C ATOM 1118 CG PHE A 425 55.660 30.152 127.112 1.00 23.69 A C ATOM 1119 CD1 PHE A 425 54.673 30.740 127.898 1.00 22.35 A C ATOM 1120 CD2 PHE A 425 55.506 28.820 126.729 1.00 21.86 A C ATOM 1121 CE1 PHE A 425 53.542 30.016 128.288 1.00 23.01 A C ATOM 1122 CE2 PHE A 425 54.379 28.086 127.113 1.00 21.25 A C ATOM 1123 CZ PHE A 425 53.395 28.684 127.892 1.00 21.91 A C ATOM 1124 C PHE A 425 55.236 32.287 125.205 1.00 29.92 A C ATOM 1125 O PHE A 425 55.177 33.475 125.525 1.00 32.27 A O ATOM 1126 N THR A 426 54.172 31.586 124.843 1.00 28.15 A N ATOM 1127 CA THR A 426 52.858 32.195 124.817 1.00 28.89 A C ATOM 1128 CB THR A 426 52.581 32.896 123.463 1.00 30.65 A C ATOM 1129 OG1 THR A 426 51.258 33.445 123.476 1.00 30.50 A O ATOM 1130 CG2 THR A 426 52.692 31.913 122.309 1.00 27.51 A C ATOM 1131 C THR A 426 51.771 31.168 125.054 1.00 28.39 A C ATOM 1132 O THR A 426 51.936 29.991 124.763 1.00 27.43 A O ATOM 1133 N GLU A 427 50.662 31.627 125.615 1.00 31.92 A N ATOM 1134 CA GLU A 427 49.515 30.767 125.864 1.00 33.81 A C ATOM 1135 CB GLU A 427 48.931 31.032 127.252 1.00 35.60 A C ATOM 1136 CO GLU A 427 49.820 30.574 128.402 1.00 41.56 A C ATOM 1137 CD GLU A 427 49.178 30.786 129.765 1.00 43.70 A C ATOM 1138 OE1 GLU A 427 48.985 31.959 130.162 1.00 45.79 A O ATOM 1139 OE2 GLU A 427 48.865 29.779 130.437 1.00 43.08 A O ATOM 1140 C GLU A 427 48.501 31.133 124.785 1.00 33.55 A C ATOM 1141 O GLU A 427 48.634 32.165 124.127 1.00 32.48 A O ATOM 1142 N GLY A 428 47.492 30.297 124.596 1.00 32.38 A N ATOM 1143 CA GLY A 428 46.509 30.596 123.575 1.00 34.96 A C ATOM 1144 C GLY A 428 47.015 30.234 122.189 1.00 35.38 A C ATOM 1145 O GLY A 428 48.137 29.740 122.050 1.00 34.55 A O ATOM 1146 N PRO A 429 46.210 30.482 121.139 1.00 35.27 A N ATOM 1147 CD PRO A 429 44.979 31.286 121.203 1.00 35.48 A C ATOM 1148 CA PRO A 429 46.555 30.185 119.744 1.00 32.90 A C ATOM 1149 CB PRO A 429 45.396 30.803 118.966 1.00 33.89 A C ATOM 1150 CG PRO A 429 44.964 31.931 119.848 1.00 34.64 A C ATOM 1151 C PRO A 429 47.913 30.740 119.329 1.00 30.15 A C ATOM 1152 O PRO A 429 48.156 31.939 119.403 1.00 32.20 A O ATOM 1153 N PRO A 430 48.817 29.858 118.886 1.00 27.85 A N ATOM 1154 CD PRO A 430 48.637 28.397 118.903 1.00 26.06 A C ATOM 1155 CA PRO A 430 50.173 30.211 118.450 1.00 27.78 A C ATOM 1156 CB PRO A 430 50.869 28.849 118.335 1.00 28.30 A C ATOM 1157 CG PRO A 430 50.029 27.927 119.193 1.00 29.20 A C ATOM 1158 C PRO A 430 50.260 30.989 117.135 1.00 27.63 A C ATOM 1159 O PRO A 430 51.068 31.909 117.000 1.00 26.32 A O ATOM 1160 N LEU A 431 49.437 30.611 116.164 1.00 26.85 A N ATOM 1161 CA LEU A 431 49.470 31.257 114.858 1.00 28.30 A C ATOM 1162 CB LEU A 431 48.752 30.395 113.815 1.00 26.29 A C ATOM 1163 CG LEU A 431 49.353 29.024 113.507 1.00 26.78 A C ATOM 1164 CD1 LEU A 431 48.615 28.430 112.326 1.00 27.79 A C ATOM 1165 CD2 LEU A 431 50.827 29.144 113.188 1.00 25.85 A C ATOM 1166 C LEU A 431 48.897 32.658 114.815 1.00 26.95 A C ATOM 1167 O LEU A 431 47.776 32.891 115.248 1.00 27.17 A O ATOM 1168 N HIS A 432 49.681 33.585 114.279 1.00 27.31 A N ATOM 1169 CA HIS A 432 49.262 34.971 114.144 1.00 29.66 A C ATOM 1170 CB HIS A 432 50.469 35.883 114.367 1.00 30.80 A C ATOM 1171 CG HIS A 432 50.157 37.342 114.263 1.00 35.25 A C ATOM 1172 CD2 HIS A 432 50.006 38.291 115.216 1.00 36.05 A C ATOM 1173 ND1 HIS A 432 49.973 37.980 113.056 1.00 35.61 A N ATOM 1174 CE1 HIS A 432 49.724 39.260 113.269 1.00 35.01 A C ATOM 1175 NE2 HIS A 432 49.739 39.474 114.571 1.00 37.63 A N ATOM 1176 C HIS A 432 48.688 35.148 112.729 1.00 31.08 A C ATOM 1177 O HIS A 432 48.989 34.353 111.843 1.00 31.29 A O ATOM 1178 N LYS A 433 47.855 36.169 112.525 1.00 30.77 A N ATOM 1179 CA LYS A 433 47.252 36.437 111.214 1.00 31.04 A C ATOM 1180 CB LYS A 433 46.590 37.817 111.186 1.00 36.69 A C ATOM 1181 CG LYS A 433 45.486 38.010 112.205 1.00 46.32 A C ATOM 1182 CD LYS A 433 45.180 39.489 112.428 1.00 52.39 A C ATOM 1183 CE LYS A 433 44.194 39.680 113.585 1.00 57.26 A C ATOM 1184 NZ LYS A 433 43.913 41.116 113.889 1.00 59.05 A N ATOM 1185 C LYS A 433 48.328 36.411 110.148 1.00 30.86 A C ATOM 1186 O LYS A 433 48.111 35.954 109.025 1.00 28.27 A O ATOM 1187 N ASP A 434 49.496 36.919 110.511 1.00 29.06 A N ATOM 1188 CA ASP A 434 50.609 36.960 109.591 1.00 26.69 A C ATOM 1189 CB ASP A 434 51.766 37.732 110.213 1.00 26.22 A C ATOM 1190 CG ASP A 434 52.923 37.905 109.258 1.00 27.32 A C ATOM 1191 OD1 ASP A 434 53.916 37.168 109.388 1.00 27.96 A O ATOM 1192 OD2 ASP A 434 52.837 38.774 108.366 1.00 29.60 A O ATOM 1193 C ASP A 434 51.052 35.557 109.202 1.00 27.04 A C ATOM 1194 O ASP A 434 51.350 35.300 108.039 1.00 26.95 A O ATOM 1195 N ASP A 435 51.086 34.644 110.169 1.00 26.04 A N ATOM 1196 CA ASP A 435 51.496 33.270 109.890 1.00 26.18 A C. ATOM 1197 CB ASP A 435 51.629 32.453 111.186 1.00 25.76 A C ATOM 1198 CG ASP A 435 52.659 33.026 112.159 1.00 23.37 A C ATOM 1199 OD1 ASP A 435 53.833 33.231 111.778 1.00 17.56 A O ATOM 1200 OD2 ASP A 435 52.281 33.257 113.319 1.00 21.37 A O ATOM 1201 C ASP A 435 50.483 32.586 108.979 1.00 26.53 A C ATOM 1202 O ASP A 435 50.857 31.854 108.065 1.00 27.59 A O ATOM 1203 N VAL A 436 49.202 32.824 109.243 1.00 26.10 A N ATOM 1204 CA VAL A 436 48.123 32.238 108.461 1.00 27.17 A C ATOM 1205 CB VAL A 436 46.758 32.516 109.116 1.00 28.67 A C ATOM 1206 CG1 VAL A 436 45.651 31.841 108.322 1.00 28.01 A C ATOM 1207 CG2 VAL A 436 46.760 32.012 110.546 1.00 27.09 A C ATOM 1208 C VAL A 436 48.105 32.755 107.021 1.00 28.36 A C ATOM 1209 O VAL A 436 47.814 32.006 106.096 1.00 28.48 A O ATOM 1210 N ASN A 437 48.411 34.034 106.832 1.00 30.05 A N ATOM 1211 CA ASN A 437 48.449 34.604 105.488 1.00 32.08 A C ATOM 1212 CB ASN A 437 48.670 36.121 105.525 1.00 36.19 A C ATOM 1213 CG ASN A 437 47.464 36.875 106.018 1.00 40.19 A C ATOM 1214 OD1 ASN A 437 46.328 36.484 105.759 1.00 44.41 A O ATOM 1215 ND2 ASN A 437 47.701 37.978 106.719 1.00 44.69 A N ATOM 1216 C ASN A 437 49.589 33.983 104.701 1.00 30.92 A C ATOM 1217 O ASN A 437 49.406 33.559 103.565 1.00 31.67 A O ATOM 1218 N GLY A 438 50.768 33.946 105.315 1.00 27.54 A N ATOM 1219 CA GLY A 438 51.931 33.385 104.659 1.00 25.40 A C ATOM 1220 C GLY A 438 51.755 31.952 104.205 1.00 24.52 A C ATOM 1221 O GLY A 438 52.171 31.593 103.110 1.00 26.30 A O ATOM 1222 N ILE A 439 51.137 31.125 105.039 1.00 23.54 A N ATOM 1223 CA ILE A 439 50.943 29.732 104.681 1.00 23.31 A C ATOM 1224 CB ILE A 439 50.619 28.871 105.944 1.00 20.22 A C ATOM 1225 CG2 ILE A 439 49.210 29.136 106.450 1.00 18.09 A C ATOM 1226 CG1 ILE A 439 50.814 27.393 105.614 1.00 21.12 A C ATOM 1227 CD1 ILE A 439 52.238 27.048 105.201 1.00 14.56 A C ATOM 1228 C ILE A 439 49.867 29.547 103.593 1.00 24.64 A C ATOM 1229 O ILE A 439 50.017 28.712 102.705 1.00 25.35 A O ATOM 1230 N ARG A 440 48.793 30.324 103.649 1.00 23.43 A N ATOM 1231 CA ARG A 440 47.751 30.217 102.638 1.00 24.74 A C ATOM 1232 CB ARG A 440 46.481 30.932 103.091 1.00 25.89 A C ATOM 1233 CG ARG A 440 45.673 30.154 104.093 1.00 28.05 A C ATOM 1234 CD ARG A 440 44.453 30.927 104.518 1.00 33.06 A C ATOM 1235 NE ARG A 440 43.678 30.183 105.502 1.00 40.49 A N ATOM 1236 CZ ARG A 440 42.752 30.722 106.286 1.00 43.77 A C ATOM 1237 NH1 ARG A 440 42.485 32.020 106.205 1.00 45.47 A N ATOM 1238 NH2 ARG A 440 42.089 29.964 107.150 1.00 43.22 A N ATOM 1239 C ARO A 440 48.217 30.806 101.312 1.00 26.05 A C ATOM 1240 O ARG A 440 47.691 30.466 100.257 1.00 29.07 A O ATOM 1241 N HIS A 441 49.201 31.694 101.360 1.00 24.35 A N ATOM 1242 CA HIS A 441 49.707 32.290 100.139 1.00 24.72 A C ATOM 1243 CB HIS A 441 50.628 33.465 100.450 1.00 21.94 A C ATOM 1244 CG HIS A 441 50.942 34.308 99.255 1.00 21.49 A C ATOM 1245 CD2 HIS A 441 52.068 34.421 98.513 1.00 23.26 A C ATOM 1246 ND1 HIS A 441 50.018 35.152 98.679 1.00 23.21 A N ATOM 1247 CE1 HIS A 441 50.561 35.748 97.634 1.00 21.93 A C ATOM 1248 NE2 HIS A 441 51.804 35.322 97.512 1.00 24.09 A N ATOM 1249 C HIS A 441 50.463 31.238 99.332 1.00 26.24 A C ATOM 1250 O HIS A 441 50.531 31.313 98.104 1.00 26.96 A O ATOM 1251 N LEU A 442 51.028 30.260 100.032 1.00 27.09 A N ATOM 1252 CA LEU A 442 51.770 29.178 99.394 1.00 27.80 A C ATOM 1253 CB LEU A 442 52.861 28.648 100.329 1.00 28.49 A C ATOM 1254 CG LEU A 442 54.042 29.552 100.679 1.00 30.92 A C ATOM 1255 CD1 LEU A 442 54.898 28.875 101.737 1.00 31.60 A C ATOM 1256 CD2 LEU A 442 54.863 29.836 99.434 1.00 31.89 A C ATOM 1257 C LEU A 442 50.877 28.009 98.984 1.00 28.59 A C ATOM 1258 O LEU A 442 51.084 27.420 97.929 1.00 28.30 A O ATOM 1259 N TYR A 443 49.896 27.674 99.821 1.00 30.49 A N ATOM 1260 CA TYR A 443 48.993 26.553 99.548 1.00 31.37 A C ATOM 1261 CB TYR A 443 49.181 25.450 100.601 1.00 30.85 A C ATOM 1262 CG TYR A 443 50.611 24.990 100.753 1.00 28.19 A C ATOM 1263 CD1 TYR A 443 51.462 25.575 101.697 1.00 25.52 A C ATOM 1264 CE1 TYR A 443 52.805 25.190 101.793 1.00 23.19 A C ATOM 1265 CD2 TYR A 443 51.133 24.007 99.913 1.00 27.48 A C ATOM 1266 CE2 TYR A 443 52.469 23.617 100.000 1.00 26.82 A C ATOM 1267 CZ TYR A 443 53.298 24.213 100.937 1.00 24.13 A C ATOM 1268 OH TYR A 443 54.618 23.837 100.986 1.00 24.42 A O ATOM 1269 C TYR A 443 47.518 26.945 99.497 1.00 31.76 A C ATOM 1270 O TYR A 443 46.719 26.112 99.036 1.00 33.61 A O ATOM 1271 OT TYR A 443 47.163 28.054 99.935 1.00 33.91 A O ATOM 2560 ZN ZN A 1 63.267 29.950 112.382 1.00 18.93 Z ZN ATOM 2561 ZN ZN A 2 70.729 19.617 111.673 1.00 22.07 Z ZN ATOM 2565 CA CA A 3 71.413 25.140 121.665 1.00 25.39 C C ATOM 2566 CA CA A 4 63.107 15.170 103.757 1.00 28.86 C C ATOM 2567 CA CA A 5 67.687 17.476 126.440 1.00 49.10 C C ATOM 2568 CA CA A 6 57.389 24.336 131.008 1.00 56.13 C C ATOM 2573 CA CA A 7 41.603 20.860 107.667 1.00 99.94 C C ATOM 2515 C1 FRA A 1 62.295 30.885 117.488 1.00 16.45 M C ATOM 2516 C2 FRA A 1 63.038 29.608 117.942 1.00 19.42 M C ATOM 2517 C3 FRA A 1 61.951 28.564 118.122 1.00 18.32 M C ATOM 2518 C4 FRA A 1 64.019 29.134 116.841 1.00 18.44 M C ATOM 2519 C5 FRA A 1 65.268 30.026 116.452 1.00 20.30 M C ATOM 2520 C6 FRA A 1 66.093 29.344 115.298 1.00 21.58 M C ATOM 2521 N7 FRA A 1 65.323 29.140 114.074 1.00 19.54 M N ATOM 2522 O8 FRA A 1 65.083 30.177 113.358 1.00 20.40 M O ATOM 2523 C9 FRA A 1 64.851 27.958 113.673 1.00 20.49 M C ATOM 2524 O10 FRA A 1 64.213 27.793 112.689 1.00 19.70 M O ATOM 2525 C11 FRA A 1 66.274 30.187 117.629 1.00 22.72 M C ATOM 2526 N12 FRA A 1 66.450 31.428 118.131 1.00 21.65 M N ATOM 2527 C13 FRA A 1 67.389 31.754 119.271 1.00 23.60 M C ATOM 2528 C14 FRA A 1 68.279 33.067 118.969 1.00 24.52 M C ATOM 2529 C15 FRA A 1 69.263 33.407 120.153 1.00 23.38 M C ATOM 2530 C16 FRA A 1 67.424 34.373 118.736 1.00 23.95 M C ATOM 2531 C17 FRA A 1 69.119 32.883 117.677 1.00 21.36 M C ATOM 2532 C18 FRA A 1 66.491 31.847 120.586 1.00 23.15 M C ATOM 2533 O19 FRA A 1 65.406 32.468 120.589 1.00 24.19 M O ATOM 2534 N20 FRA A 1 67.003 31.196 121.667 1.00 21.19 M N ATOM 2535 C21 FRA A 1 66.350 31.137 122.996 1.00 25.36 M C ATOM 2536 O22 FRA A 1 66.882 29.180 118.067 1.00 22.29 M O ATOM 1273 CB ASP B 110 39.115 26.293 159.737 1.00 61.05 B C ATOM 1274 CG ASP B 110 39.042 27.399 160.776 1.00 62.86 B C ATOM 1275 OD1 ASP B 110 40.101 27.786 161.322 1.00 62.33 B O ATOM 1276 OD2 ASP B 110 37.917 27.876 161.046 1.00 63.37 B O ATOM 1277 C ASP B 110 40.865 24.867 160.849 1.00 56.49 B C ATOM 1278 O ASP B 110 41.355 25.782 161.519 1.00 56.57 B O ATOM 1279 N ASP B 110 38.439 24.617 161.434 1.00 58.69 B N ATOM 1280 CA ASP B 110 39.418 24.920 160.351 1.00 58.71 B C ATOM 1281 N LEU B 111 41.541 23.778 160.512 1.00 52.64 B N ATOM 1282 CA LEU B 111 42.921 23.579 160.910 1.00 48.28 B C ATOM 1283 CB LEU B 111 43.265 22.094 160.794 1.00 48.88 B C ATOM 1284 CG LEU B 111 44.509 21.605 161.528 1.00 50.33 B C ATOM 1285 CD1 LEU B 111 44.535 22.156 162.948 1.00 50.73 B C ATOM 1286 CD2 LEU B 111 44.500 20.088 161.540 1.00 51.89 B C ATOM 1287 C LEU B 111 43.846 24.419 160.029 1.00 43.58 B C ATOM 1288 O LEU B 111 43.584 24.607 158.838 1.00 42.86 B O ATOM 1289 N LYS B 112 44.917 24.942 160.615 1.00 37.78 B N ATOM 1290 CA LYS B 112 45.858 25.745 159.846 1.00 34.84 B C ATOM 1291 CB LYS B 112 45.341 27.176 159.702 1.00 35.26 B C ATOM 1292 CG LYS B 112 45.439 28.007 160.972 1.00 39.03 B C ATOM 1293 CD LYS B 112 45.160 29.466 160.674 1.00 38.56 B C ATOM 1294 CE LYS B 112 45.529 30.353 161.845 1.00 41.04 B C ATOM 1295 NZ LYS B 112 45.396 31.790 161.475 1.00 41.35 B N ATOM 1296 C LYS B 112 47.233 25.767 160.498 1.00 32.44 B C ATOM 1297 O LYS B 112 47.395 25.317 161.628 1.00 31.94 B O ATOM 1298 N TRP B 113 48.225 26.284 159.779 1.00 30.35 B N ATOM 1299 CA TRP B 113 49.571 26.359 160.320 1.00 30.31 B C ATOM 1300 CB TRP B 113 50.613 26.516 159.204 1.00 27.93 B C ATOM 1301 CG TRP B 113 50.690 25.351 158.258 1.00 27.86 B C ATOM 1302 CD2 TRP B 113 51.204 24.040 158.541 1.00 26.96 B C ATOM 1303 CE2 TRP B 113 51.058 23.271 157.363 1.00 27.Z9 B C ATOM 1304 CE3 TRP B 113 51.773 23.441 159.674 1.00 23.04 B C ATOM 1305 CD1 TRP B 113 50.266 25.321 156.958 1.00 26.75 B C ATOM 1306 NE1 TRP B 113 50.483 24.078 156.415 1.00 23.61 B N ATOM 1307 CZ2 TRP B 113 51.460 21.930 157.287 1.00 24.46 B C ATOM 1308 CZ3 TRP B 113 52.171 22.108 159.597 1.00 23.32 B C ATOM 1309 CH2 TRP B 113 52.012 21.369 158.410 1.00 23.78 B C ATOM 1310 C TRP B 113 49.645 27.558 161.252 1.00 31.82 B C ATOM 1311 O TRP B 113 49.024 28.589 160.996 1.00 32.51 B O ATOM 1312 N HIS B 114 50.400 27.419 162.335 1.00 31.20 B N ATOM 1313 CA HIS B 114 50.549 28.507 163.285 1.00 31.82 B C ATOM 1314 CB HIS B 114 50.577 27.963 164.711 1.00 31.55 B C ATOM 1315 CG HIS B 114 49.237 27.513 165.193 1.00 32.54 B C ATOM 1316 CD2 HIS B 114 47.999 27.711 164.681 1.00 32.52 B C ATOM 1317 ND1 HIS B 114 49.064 26.767 166.337 1.00 33.18 B N ATOM 1318 CE1 HIS B 114 47.777 26.523 166.510 1.00 32.64 B C ATOM 1319 NE2 HIS B 114 47.110 27.085 165.518 1.00 34.29 B N ATOM 1320 C HIS B 114 51.774 29.357 163.006 1.00 30.66 B C ATOM 1321 O HIS B 114 51.997 30.358 163.679 1.00 34.99 B O ATOM 1322 N HIS B 115 52.572 28.950 162.022 1.00 28.55 B N ATOM 1323 CA HIS B 115 53.745 29.722 161.617 1.00 25.56 B C ATOM 1324 CB HIS B 115 55.044 28.934 161.824 1.00 25.76 B C ATOM 1325 CG HIS B 115 55.057 27.591 161.164 1.00 25.72 B C ATOM 1326 CD2 HIS B 115 55.839 27.090 160.180 1.00 24.52 B C ATOM 1327 ND1 HIS B 115 54.198 26.576 161.526 1.00 24.79 B N ATOM 1328 CE1 HIS B 115 54.453 25.506 160.796 1.00 22.93 B C ATOM 1329 NE2 HIS B 115 55.445 25.791 159.971 1.00 23.07 B N ATOM 1330 C HIS B 115 53.553 30.058 160.144 1.00 25.78 B C ATOM 1331 O HIS B 115 52.775 29.406 159.456 1.00 26.11 B O ATOM 1332 N HIS B 116 54.261 31.072 159.666 1.00 25.82 B N ATOM 1333 CA HIS B 116 54.133 31.514 158.286 1.00 25.15 B C ATOM 1334 CB HIS B 116 53.911 33.030 158.253 1.00 25.12 B C ATOM 1335 CG HIS B 116 52.559 33.446 158.740 1.00 26.86 B C ATOM 1336 CD2 HIS B 116 51.495 32.712 159.144 1.00 25.46 B C ATOM 1337 ND1 HIS B 116 52.177 34.766 158.840 1.00 26.98 B N ATOM 1338 CE1 HIS B 116 50.934 34.826 159.285 1.00 29.50 B C ATOM 1339 NE2 HIS B 116 50.498 33.594 159.477 1.00 28.22 B N ATOM 1340 C HIS B 116 55.290 31.152 157.372 1.00 24.84 B C ATOM 1341 O HIS B 116 55.163 31.228 156.155 1.00 24.51 B O ATOM 1342 N ASN B 117 56.421 30.779 157.955 1.00 23.92 B N ATOM 1343 CA ASN B 117 57.581 30.395 157.166 1.00 23.42 B C ATOM 1344 CB ASN B 117 58.868 30.914 157.824 1.00 24.61 B C ATOM 1345 CG ASN B 117 59.019 30.486 159.285 1.00 27.08 B C ATOM 1346 OD1 ASN B 117 58.047 30.395 160.041 1.00 28.75 B O ATOM 1347 ND2 ASN B 117 60.259 30.244 159.689 1.00 24.54 B N ATOM 1348 C ASN B 117 57.568 28.878 157.046 1.00 23.79 B C ATOM 1349 O ASN B 117 58.249 28.160 157.779 1.00 22.99 B O ATOM 1350 N ILE B 118 56.760 28.401 156.107 1.00 23.12 B N ATOM 1351 CA ILE B 118 56.585 26.9791 55.876 1.00 24.05 B C ATOM 1352 CB ILE B 118 55.245 26.7341 55.156 1.00 25.87 B C ATOM 1353 CG2 ILE B 118 55.066 25.2561 54.855 1.00 25.54 B C ATOM 1354 CG1 ILE B 118 54.104 27.259 156.039 1.00 26.83 B C ATOM 1355 CD1 ILE B 118 52.721 27.053 155.465 1.00 31.75 B C ATOM 1356 C ILE B 118 57.722 26.340 155.097 1.00 23.08 B C ATOM 1357 O ILE B 118 58.319 26.962 154.223 1.00 25.00 B O ATOM 1358 N THR B 119 58.029 25.094 155.429 1.00 21.12 B N ATOM 1359 CA THR B 119 59.096 24.382 154.744 1.00 19.30 B C ATOM 1360 CB THR B 119 60.203 23.938 155.721 1.00 18.41 B C ATOM 1361 OG1 THR B 119 59.640 23.097 156.732 1.00 18.81 B O ATOM 1362 CG2 THR B 119 60.861 25.147 156.359 1.00 14.91 B C ATOM 1363 C THR B 119 58.564 23.156 154.026 1.00 18.87 B C ATOM 1364 O THR B 119 57.539 22.586 154.415 1.00 17.08 B O ATOM 1365 N TYR B 120 59.260 22.756 152.966 1.00 18.82 B N ATOM 1366 CA TYR B 120 58.848 21.584 152.207 1.00 17.71 B C ATOM 1367 CB TYR B 120 57.966 21.973 151.004 1.00 14.12 B C ATOM 1368 CG TYR B 120 58.671 22.725 149.891 1.00 14.85 B C ATOM 1369 CD1 TYR B 120 58.811 24.113 149.936 1.00 15.43 B C ATOM 1370 CE1 TYR B 120 59.392 24.817 148.882 1.00 12.87 B C ATOM 1371 CD2 TYR B 120 59.144 22.052 148.761 1.00 15.15 B C ATOM 1372 CE2 TYR B 120 59.725 22.746 147.702 1.00 15.56 B C ATOM 1373 CZ TYR B 120 59.842 24.126 147.766 1.00 17.67 B C ATOM 1374 OH TYR B 120 60.378 24.816 146.702 1.00 20.47 B O ATOM 1375 C TYR B 120 60.048 20.798 151.726 1.00 14.81 B C ATOM 1376 O TYR B 120 61.116 21.353 151.497 1.00 14.65 B O ATOM 1377 N TRP B 121 59.840 19.499 151.567 1.00 12.91 B N ATOM 1378 CA TRP B 121 60.867 18.587 151.121 1.00 14.27 B C ATOM 1379 CB TRP B 121 61.271 17.677 152.295 1.00 16.23 B C ATOM 1380 CG TRP B 121 62.237 16.559 151.970 1.00 16.27 B C ATOM 1381 CD2 TRP B 121 62.292 15.266 152.595 1.00 17.47 B C ATOM 1382 GE2 TRP B 121 63.424 14.600 152.078 1.00 17.45 B C ATOM 1383 CE3 TRP B 121 61.496 14.610 153.548 1.00 17.63 B C ATOM 1384 CD1 TRP B 121 63.303 16.613 151.117 1.00 17.04 B C ATOM 1385 NE1 TRP B 121 64.021 15.442 151.179 1.00 16.74 B N ATOM 1386 CZ2 TRP B 121 63.783 13.307 152.484 1.00 18.60 B C ATOM 1387 CZ3 TRP B 121 61.853 13.327 153.952 1.00 18.18 B C ATOM 1388 CH2 TRP B 121 62.988 12.691 153.420 1.00 18.22 B C ATOM 1389 C TRP B 121 60.355 17.741 149.955 1.00 15.49 B C ATOM 1390 O TRP B 121 59.312 17.093 150.061 1.00 13.62 B O ATOM 1391 N ILE B 122 61.086 17.770 148.841 1.00 12.10 B N ATOM 1392 CA ILE B 122 60.729 16.956 147.696 1.00 13.59 B C ATOM 1393 CB ILE B 122 61.167 17.608 146.381 1.00 14.78 B C ATOM 1394 CG2 ILE B 122 60.773 16.715 145.214 1.00 10.29 B C ATOM 1395 CG1 ILE B 122 60.520 18.991 146.254 1.00 13.64 B C ATOM 1396 CD1 ILE B 122 61.024 19.811 145.080 1.00 12.29 B C ATOM 1397 C ILE B 122 61.514 15.672 147.918 1.00 13.64 B C ATOM 1398 O ILE B 122 62.694 15.588 147.592 1.00 14.54 B O ATOM 1399 N GLN B 123 60.855 14.679 148.496 1.00 13.68 B N ATOM 1400 CA GLN B 123 61.496 13.413 148.802 1.00 15.77 B C ATOM 1401 CB GLN B 123 60.564 12.573 149.662 1.00 14.28 B C ATOM 1402 CG GLN B 123 61.092 11.200 149.957 1.00 19.68 B C ATOM 1403 CD GLN B 123 60.133 10.402 150.794 1.00 22.52 B C ATOM 1404 OE1 GLN B 123 59.933 9.211 150.560 1.00 28.95 B O ATOM 1405 NE2 GLN B 123 59.534 11.048 151.782 1.00 19.79 B N ATOM 1406 C GLN B 123 61.971 12.587 147.604 1.00 18.55 B C ATOM 1407 O GLN B 123 63.086 12.069 147.611 1.00 18.76 B O ATOM 1408 N ASN B 124 61.118 12.428 146.596 1.00 19.57 B N ATOM 1409 CA ASN B 124 61.492 11.664 145.412 1.00 17.91 B C ATOM 1410 CB ASN B 124 61.111 10.184 145.549 1.00 17.29 B C ATOM 1411 CG ASN B 124 59.628 9.965 145.734 1.00 18.23 B C ATOM 1412 OD1 ASN B 124 58.830 10.882 145.602 1.00 20.83 B O ATOM 1413 ND2 ASN B 124 59.254 8.735 146.035 1.00 18.51 B N ATOM 1414 C ASN B 124 60.868 12.265 144.165 1.00 19.24 B C ATOM 1415 O ASN B 124 60.138 13.261 144.239 1.00 19.36 B O ATOM 1416 N TYR B 125 61.164 11.666 143.016 1.00 18.73 B N ATOM 1417 CA TYR B 125 60.670 12.187 141.749 1.00 14.58 B C ATOM 1418 CB TYR B 125 61.844 12.731 140.921 1.00 15.39 B C ATOM 1419 CG TYR B 125 62.538 13.932 141.536 1.00 13.70 B C ATOM 1420 CD1 TYR B 125 63.526 13.777 142.510 1.00 12.60 B C ATOM 1421 CE1 TYR B 125 64.113 14.889 143.124 1.00 11.44 B C ATOM 1422 CD2 TYR B 125 62.156 15.229 141.187 1.00 15.12 B C ATOM 1423 CE2 TYR B 125 62.731 16.341 141.793 1.00 11.78 B C ATOM 1424 CZ TYR B 125 63.706 16.164 142.760 1.00 13.63 B C ATOM 1425 OH TYR B 125 64.257 17.270 143.365 1.00 11.62 B O ATOM 1426 C TYR B 125 59.890 11.203 140.899 1.00 14.07 B C ATOM 1427 O TYR B 125 59.880 10.005 141.158 1.00 12.64 B O ATOM 1428 N SER B 126 59.230 11.737 139.877 1.00 15.52 B N ATOM 1429 CA SER B 126 58.461 10.929 138.936 1.00 17.11 B C ATOM 1430 CB SER B 126 57.246 11.705 138.419 1.00 17.11 B C ATOM 1431 OG SER B 126 56.716 11.100 137.252 1.00 14.91 B O ATOM 1432 C SER B 126 59.374 10.596 137.766 1.00 20.19 B C ATOM 1433 O SER B 126 60.298 11.345 137.452 1.00 19.00 B O ATOM 1434 N GLU B 127 59.109 9.480 137.108 1.00 23.95 B N ATOM 1435 CA GLU B 127 59.937 9.079 135.982 1.00 27.98 B C ATOM 1436 CB GLU B 127 59.795 7.575 135.743 1.00 33.47 B C ATOM 1437 CG GLU B 127 59.913 6.740 137.004 1.00 40.62 B C ATOM 1438 CD GLU B 127 60.077 5.255 136.718 1.00 45.97 B C ATOM 1439 OE1 GLU B 127 61.082 4.880 136.068 1.00 47.09 B O ATOM 1440 OE2 GLU B 127 59.204 4.466 137.148 1.00 47.02 B O ATOM 1441 C GLU B 127 59.585 9.825 134.700 1.00 26.19 B C ATOM 1442 O GLU B 127 60.331 9.763 133.732 1.00 27.48 B O ATOM 1443 N ASP B 128 58.464 10.543 134.702 1.00 23.99 B N ATOM 1444 CA ASP B 128 58.008 11.256 133.511 1.00 21.74 B C ATOM 1445 CB ASP B 128 56.496 11.480 133.557 1.00 22.01 B C ATOM 1446 CG ASP B 128 55.717 10.228 133.884 1.00 18.40 B C ATOM 1447 OD1 ASP B 128 56.138 9.119 133.514 1.00 21.04 B O ATOM 1448 OD2 ASP B 128 54.652 10.371 134.504 1.00 17.97 B O ATOM 1449 C ASP B 128 58.637 12.606 133.194 1.00 22.03 B C ATOM 1450 O ASP B 128 58.578 13.052 132.051 1.00 21.61 B O ATOM 1451 N LEU B 129 59.207 13.273 134.189 1.00 19.22 B N ATOM 1452 CA LEU B 129 59.797 14.582 133.953 1.00 17.22 B C ATOM 1453 CB LEU B 129 58.887 15.664 134.528 1.00 16.52 B C ATOM 1454 CG LEU B 129 57.497 15.796 133.901 1.00 20.26 B C ATOM 1455 CD1 LEU B 129 56.642 16.745 134.732 1.00 18.39 B C ATOM 1456 CD2 LEU B 129 57.629 16.303 132.471 1.00 19.31 B C ATOM 1457 C LEU B 129 61.179 14.713 134.566 1.00 17.81 B C ATOM 1458 O LEU B 129 61.515 14.000 135.511 1.00 20.83 B O ATOM 1459 N PRO B 130 62.014 15.617 134.021 1.00 17.25 B N ATOM 1460 CD PRO B 130 61.811 16.408 132.796 1.00 15.36 B C ATOM 1461 CA PRO B 130 63.371 15.820 134.557 1.00 17.25 B C ATOM 1462 CB PRO B 130 64.002 16.790 133.554 1.00 14.93 B C ATOM 1463 CG PRO B 130 63.214 16.559 132.292 1.00 15.96 B C ATOM 1464 C PRO B 130 63.250 16.450 135.954 1.00 15.64 B C ATOM 1465 O PRO B 130 62.245 17.096 136.250 1.00 15.44 B O ATOM 1466 N ARG B 131 64.259 16.265 136.805 1.00 16.42 B N ATOM 1467 CA ARG B 131 64.237 16.840 138.159 1.00 16.86 B C ATOM 1468 CB ARG B 131 65.551 16.591 138.906 1.00 18.20 B C ATOM 1469 CG ARG B 131 65.708 15.207 139.469 1.00 22.57 B C ATOM 1470 CD ARG B 131 66.845 15.143 140.470 1.00 21.69 B C ATOM 1471 NE ARG B 131 67.022 13.771 140.932 1.00 26.97 B N ATOM 1472 CZ ARG B 131 67.541 13.427 142.107 1.00 28.81 B C ATOM 1473 NH1 ARG B 131 67.945 14.360 142.966 1.00 24.33 B N ATOM 1474 NH2 ARG B 131 67.641 12.143 142.424 1.00 28.78 B N ATOM 1475 C ARG B 131 64.022 18.338 138.138 1.00 16.07 B C ATOM 1476 O ARG B 131 63.219 18.869 138.899 1.00 15.45 B O ATOM 1477 N ALA B 132 64.764 19.013 137.268 1.00 14.39 B N ATOM 1478 CA ALA B 132 64.685 20.461 137.163 1.00 16.40 B C ATOM 1479 CB ALA B 132 65.677 20.959 136.106 1.00 17.38 B C ATOM 1480 C ALA B 132 63.278 20.946 136.837 1.00 16.67 B C ATOM 1481 O ALA B 132 62.844 21.984 137.326 1.00 18.93 B O ATOM 1482 N VAL B 133 62.566 20.192 136.008 1.00 15.47 B N ATOM 1483 CA VAL B 133 61.213 20.562 135.626 1.00 13.65 B C ATOM 1484 CB VAL B 133 60.721 19.694 134.433 1.00 14.12 B C ATOM 1485 CG1 VAL B 133 59.229 19.926 134.177 1.00 9.73 B C ATOM 1486 CG2 VAL B 133 61.530 20.037 133.190 1.00 12.36 B C ATOM 1487 C VAL B 133 60.259 20.394 136.803 1.00 14.22 B C ATOM 1488 O VAL B 133 59.362 21.211 137.016 1.00 13.15 B O ATOM 1489 N ILE B 134 60.460 19.323 137.563 1.00 15.06 B N ATOM 1490 CA ILE B 134 59.617 19.029 138.709 1.00 13.17 B C ATOM 1491 CB ILE B 134 59.855 17.580 139.200 1.00 14.87 B C ATOM 1492 CG2 ILE B 134 59.229 17.371 140.571 1.00 14.89 B C ATOM 1493 CG1 ILE B 134 59.287 16.597 138.166 1.00 11.36 B C ATOM 1494 CD1 ILE B 134 59.476 15.131 138.521 1.00 11.57 B C ATOM 1495 C ILE B 134 59.862 20.025 139.830 1.00 15.99 B C ATOM 1496 O ILE B 134 58.908 20.543 140.404 1.00 16.24 B O ATOM 1497 N ASP B 135 61.132 20.308 140.134 1.00 15.66 B N ATOM 1498 CA ASP B 135 61.447 21.279 141.184 1.00 15.15 B C ATOM 1499 CB ASP B 135 62.959 21.544 141.288 1.00 12.56 B C ATOM 1500 CG ASP B 135 63.746 20.351 141.803 1.00 10.35 B C ATOM 1501 OD1 ASP B 135 63.156 19.399 142.353 1.00 11.63 B O ATOM 1502 OD2 ASP B 135 64.983 20.371 141.664 1.00 17.25 B O ATOM 1503 C ASP B 135 60.752 22.603 140.871 1.00 15.48 B C ATOM 1504 O ASP B 135 60.095 23.187 141.732 1.00 20.45 B O ATOM 1505 N ASP B 136 60.902 23.069 139.635 1.00 14.76 B N ATOM 1506 CA ASP B 136 60.313 24.328 139.189 1.00 13.88 B C ATOM 1507 CB ASP B 136 60.768 24.621 137.762 1.00 16.77 B C ATOM 1508 CG ASP B 136 60.207 25.919 137.221 1.00 19.24 B C ATOM 1509 OD1 ASP B 136 60.611 26.985 137.721 1.00 20.16 B O ATOM 1510 OD2 ASP B 136 59.362 25.870 136.297 1.00 18.28 B O ATOM 1511 C ASP B 136 58.785 24.354 139.267 1.00 13.68 B C ATOM 1512 O ASP B 136 58.200 25.343 139.697 1.00 18.58 B O ATOM 1513 N ALA B 137 58.135 23.276 138.850 1.00 12.86 B N ATOM 1514 CA ALA B 137 56.679 23.204 138.907 1.00 10.91 B C ATOM 1515 CB ALA B 137 56.196 21.882 138.315 1.00 9.57 B C ATOM 1516 C ALA B 137 56.174 23.343 140.347 1.00 13.69 B C ATOM 1517 O ALA B 137 55.184 24.034 140.601 1.00 14.16 B O ATOM 1518 N PHE B 138 56.831 22.668 141.289 1.00 15.83 B N ATOM 1519 CA PHE B 138 56.425 22.758 142.694 1.00 16.29 B C ATOM 1520 CB PHE B 138 57.182 21.737 143.559 1.00 13.24 B C ATOM 1521 CG PHE B 138 56.731 20.304 143.363 1.00 12.26 B C ATOM 1522 CD1 PHE B 138 55.409 20.007 143.025 1.00 13.72 B C ATOM 1523 CD2 PHE B 138 57.628 19.251 143.516 1.00 9.81 B C ATOM 1524 CE1 PHE B 138 54.995 18.679 142.841 1.00 13.46 B C ATOM 1525 CE2 PHE B 138 57.224 17.927 143.337 1.00 7.35 B C ATOM 1526 CZ PHE B 138 55.907 17.641 142.998 1.00 11.80 B C ATOM 1527 C PHE B 138 56.670 24.172 143.226 1.00 16.78 B C ATOM 1528 O PHE B 138 55.871 24.709 143.990 1.00 19.28 B O ATOM 1529 N ALA B 139 57.772 24.783 142.807 1.00 17.38 B N ATOM 1530 CA ALA B 139 58.093 26.136 143.246 1.00 17.57 B C ATOM 1531 CB ALA B 139 59.490 26.521 142.770 1.00 14.41 B C ATOM 1532 C ALA B 139 57.061 27.149 142.738 1.00 18.95 B C ATOM 1533 O ALA B 139 56.664 28.060 143.467 1.00 19.80 B O ATOM 1534 N ARG B 140 56.628 26.993 141.490 1.00 19.15 B N ATOM 1535 CA ARG B 140 55.642 27.906 140.917 1.00 17.98 B C ATOM 1536 CE ARG B 140 55.596 27.761 139.388 1.00 16.03 B C ATOM 1537 CG ARG B 140 56.888 28.201 138.707 1.00 16.18 B C ATOM 1538 CD ARG B 140 56.812 28.138 137.181 1.00 18.32 B C ATOM 1539 NE ARG B 140 56.746 26.768 136.685 1.00 14.27 B N ATOM 1540 CZ ARG B 140 55.666 26.213 136.150 1.00 14.50 B C ATOM 1541 NH1 ARG B 140 54.548 26.912 136.030 1.00 12.39 B N ATOM 1542 NH2 ARG B 140 55.701 24.946 135.753 1.00 14.50 B N ATOM 1543 C ARG B 140 54.274 27.638 141.531 1.00 18.29 B C ATOM 1544 O ARG B 140 53.451 28.544 141.661 1.00 22.02 B O ATOM 1545 N ALA B 141 54.036 26.392 141.927 1.00 17.80 B N ATOM 1546 CA ALA B 141 52.768 26.030 142.552 1.00 17.21 B C ATOM 1547 CB ALA B 141 52.656 24.520 142.660 1.00 17.90 B C ATOM 1548 C ALA B 141 52.660 26.677 143.941 1.00 19.87 B C ATOM 1549 O ALA B 141 51.572 27.056 144.369 1.00 19.56 B O ATOM 1550 N PHE B 142 53.787 26.795 144.645 1.00 20.99 B N ATOM 1551 CA PHE B 142 53.798 27.427 145.970 1.00 21.67 B C ATOM 1552 CB PHE B 142 55.072 27.069 146.759 1.00 18.85 B C ATOM 1553 CG PHE B 142 55.008 25.734 147.446 1.00 16.57 B C ATOM 1554 CD1 PHE B 142 53.976 25.449 148.333 1.00 14.21 B C ATOM 1555 CD2 PHE B 142 55.974 24.764 147.204 1.00 14.86 B C ATOM 1556 CE1 PHE B 142 53.904 24.220 148.972 1.00 18.27 B C ATOM 1557 CE2 PHE B 142 55.917 23.527 147.836 1.00 19.57 B C ATOM 1558 CZ PHE B 142 54.879 23.251 148.724 1.00 20.55 B C ATOM 1559 C PHE B 142 53.719 28.942 145.832 1.00 21.95 B C ATOM 1560 O PHE B 142 53.101 29.613 146.652 1.00 25.86 B O ATOM 1561 N ALA B 143 54.356 29.481 144.802 1.00 20.87 B N ATOM 1562 CA ALA B 143 54.344 30.921 144.576 1.00 21.45 B C ATOM 1563 CB ALA B 143 55.222 31.268 143.390 1.00 17.43 B C ATOM 1564 C ALA B 143 52.930 31.466 144.360 1.00 23.06 B C ATOM 1565 O ALA B 143 52.661 32.629 144.658 1.00 25.48 B O ATOM 1566 N LEU B 144 52.029 30.636 143.841 1.00 24.74 B N ATOM 1567 CA LEU B 144 50.652 31.075 143.615 1.00 26.04 B C ATOM 1568 CB LEU B 144 49.797 29.958 143.010 1.00 24.21 B C ATOM 1569 CG LEU B 144 49.951 29.560 141.539 1.00 27.50 B C ATOM 1570 CD1 LEU B 144 48.945 28.468 141.230 1.00 25.16 B C ATOM 1571 CD2 LEU B 144 49.718 30.754 140.630 1.00 23.79 B C ATOM 1572 C LEU B 144 50.020 31.481 144.934 1.00 28.47 B C ATOM 1573 O LEU B 144 49.343 32.500 145.030 1.00 30.66 B O ATOM 1574 N TRP B 145 50.245 30.664 145.951 1.00 28.49 B N ATOM 1575 CA TRP B 145 49.680 30.913 147.265 1.00 29.54 B C ATOM 1576 CB TRP B 145 49.652 29.609 148.053 1.00 26.39 B C ATOM 1577 CG TRP B 145 48.796 28.553 147.417 1.00 24.57 B C ATOM 1578 CD2 TRP B 145 47.366 28.550 147.330 1.00 25.64 B C ATOM 1579 CE2 TRP B 145 46.986 27.320 146.747 1.00 24.80 B C ATOM 1580 CR3 TRP B 145 46.366 29.464 147.695 1.00 25.42 B C ATOM 1581 CD1 TRP B 145 49.214 27.369 146.885 1.00 22.40 B C ATOM 1582 NR1 TRP B 145 48.133 26.619 146.483 1.00 22.24 B N ATOM 1583 CZ2 TRP B 145 45.644 26.977 146.522 1.00 27.07 B C ATOM 1584 CZ3 TRP B 145 45.029 29.122 147.471 1.00 26.11 B C ATOM 1585 CH2 TRP B 145 44.684 27.889 146.892 1.00 24.97 B C ATOM 1586 C TRP B 145 50.397 31.995 148.064 1.00 28.97 B C ATOM 1587 O TRP B 145 49.752 32.844 148.674 1.00 29.64 B O ATOM 1588 N SER B 146 51.724 31.979 148.063 1.00 30.94 B N ATOM 1589 CA SER B 146 52.474 32.986 148.808 1.00 33.11 B C ATOM 1590 CB SER B 146 53.967 32.675 148.776 1.00 31.16 B C ATOM 1591 OG SER B 146 54.465 32.773 147.457 1.00 34.33 B O ATOM 1592 C SER B 146 52.241 34.372 148.221 1.00 35.39 B C ATOM 1593 O SER B 146 52.600 35.381 148.827 1.00 38.15 B O ATOM 1594 N ALA B 147 51.641 34.418 147.039 1.00 35.46 B N ATOM 1595 CA ALA B 147 51.379 35.683 146.374 1.00 35.64 B C ATOM 1596 CB ALA B 147 51.187 35.457 144.883 1.00 35.78 B C ATOM 1597 C ALA B 147 50.160 36.380 146.949 1.00 36.30 B C ATOM 1598 O ALA B 147 50.054 37.600 146.875 1.00 35.93 B O ATOM 1599 N VAL B 148 49.238 35.611 147.519 1.00 36.26 B N ATOM 1600 CA VAL B 148 48.031 36.196 148.089 1.00 37.29 B C ATOM 1601 CB VAL B 148 46.761 35.601 147.435 1.00 37.45 B C ATOM 1602 CG1 VAL B 148 46.728 35.952 145.959 1.00 39.35 B C ATOM 1603 CG2 VAL B 148 46.735 34.099 147.614 1.00 37.42 B C ATOM 1604 C VAL B 148 47.926 36.035 149.606 1.00 37.54 B C ATOM 1605 O VAL B 148 46.838 36.144 150.173 1.00 38.76 B O ATOM 1606 N THR B 149 49.057 35.774 150.257 1.00 36.72 B N ATOM 1607 CA THR B 149 49.098 35.611 151.711 1.00 34.50 B C ATOM 1608 CB THR B 149 48.815 34.159 152.139 1.00 32.69 B C ATOM 1609 OG1 THR B 149 49.872 33.313 151.672 1.00 34.10 B O ATOM 1610 CG2 THR B 149 47.492 33.677 151.587 1.00 33.09 B C ATOM 1611 C THR B 149 50.484 35.975 152.241 1.00 34.43 B C ATOM 1612 O THR B 149 51.424 36.166 151.466 1.00 33.86 B O ATOM 1613 N PRO B 150 50.624 36.084 153.576 1.00 35.88 B N ATOM 1614 CD PRO B 150 49.542 36.096 154.582 1.00 36.97 B C ATOM 1615 CA PRO B 150 51.909 36.423 154.199 1.00 35.29 B C ATOM 1616 CB PRO B 150 51.491 36.993 155.548 1.00 33.79 B C ATOM 1617 CG PRO B 150 50.313 36.136 155.894 1.00 36.98 B C ATOM 1618 C PRO B 150 52.810 35.190 154.341 1.00 33.55 B C ATOM 1619 O PRO B 150 53.889 35.259 154.928 1.00 33.85 B O ATOM 1620 N LEU B 151 52.357 34.064 153.796 1.00 32.24 B N ATOM 1621 CA LEU B 151 53.111 32.813 153.850 1.00 29.72 B C ATOM 1622 CB LEU B 151 52.210 31.634 153.485 1.00 28.34 B C ATOM 1623 CG LEU B 151 50.920 31.386 154.263 1.00 29.72 B C ATOM 1624 CD1 LEU B 151 50.115 30.308 153.547 1.00 25.73 B C ATOM 1625 CD2 LEU B 151 51.241 30.971 155.697 1.00 27.68 B C ATOM 1626 C LEU B 151 54.301 32.796 152.897 1.00 28.80 B C ATOM 1627 O LEU B 151 54.253 33.384 151.817 1.00 29.79 B O ATOM 1628 N THR B 152 55.370 32.123 153.307 1.00 26.47 B N ATOM 1629 CA THR B 152 56.550 31.968 152.468 1.00 26.48 B C ATOM 1630 CB THR B 152 57.786 32.697 153.018 1.00 25.05 B C ATOM 1631 OG1 THR B 152 58.199 32.092 154.250 1.00 26.56 B O ATOM 1632 CG2 THR B 152 57.478 34.161 153.235 1.00 26.91 B C ATOM 1633 C THR B 152 56.822 30.469 152.444 1.00 27.63 B C ATOM 1634 O THR B 152 56.361 29.731 153.321 1.00 28.65 B O ATOM 1635 N PHE B 153 57.561 30.020 151.438 1.00 26.34 B N ATOM 1636 CA PHE B 153 57.858 28.603 151.289 1.00 24.22 B C ATOM 1637 CB PHE B 153 57.010 28.041 150.147 1.00 21.10 B C ATOM 1638 CG PHE B 153 55.531 28.101 150.419 1.00 21.18 B C ATOM 1639 CD1 PHE B 153 54.916 27.141 151.229 1.00 19.72 B C ATOM 1640 CD2 PHE B 153 54.761 29.150 149.924 1.00 18.40 B C ATOM 1641 CE1 PHE B 153 53.560 27.231 151.541 1.00 18.13 B C ATOM 1642 CE2 PHE B 153 53.404 29.249 150.231 1.00 15.81 B C ATOM 1643 CZ PHE B 153 52.803 28.291 151.040 1.00 17.61 B C ATOM 1644 C PHE B 153 59.338 28.362 151.045 1.00 23.36 B C ATOM 1645 O PHE B 153 59.910 28.853 150.079 1.00 25.84 B O ATOM 1646 N THR B 154 59.951 27.596 151.938 1.00 24.03 B N ATOM 1647 CA THR B 154 61.375 27.302 151.858 1.00 22.52 B C ATOM 1648 CB THR B 154 62.075 27.739 153.149 1.00 21.34 B C ATOM 1649 OG1 THR B 154 61.867 29.138 153.328 1.00 25.73 B O ATOM 1650 CG2 THR B 154 63.567 27.461 153.091 1.00 20.97 B C ATOM 1651 C THR B 154 61.629 25.824 151.638 1.00 21.11 B C ATOM 1652 O THR B 154 61.050 24.977 152.317 1.00 21.31 B O ATOM 1653 N ARG B 155 62.502 25.521 150.688 1.00 21.15 B N ATOM 1654 CA ARG B 155 62.831 24.138 150.385 1.00 21.88 B C ATOM 1655 CB ARG B 155 63.248 23.996 148.919 1.00 23.11 B C ATOM 1656 CG ARG B 155 63.532 22.559 148.524 1.00 20.37 B C ATOM 1657 CD ARG B 155 64.052 22.459 147.121 1.00 21.66 B C ATOM 1658 NE ARG B 155 64.381 21.083 146.772 1.00 18.52 B N ATOM 1659 CZ ARG B 155 64.905 20.721 145.610 1.00 17.45 B C ATOM 1660 NH1 ARG B 155 65.158 21.637 144.689 1.00 16.66 B N ATOM 1661 NH2 ARG B 155 65.174 19.447 145.372 1.00 15.63 B N ATOM 1662 C ARG B 155 63.963 23.657 151.284 1.00 22.35 B C ATOM 1663 O ARG B 155 64.973 24.341 151.435 1.00 23.68 B O ATOM 1664 N VAL B 156 63.784 22.486 151.888 1.00 21.22 B N ATOM 1665 CA VAL B 156 64.795 21.904 152.760 1.00 21.38 B C ATOM 1666 CB VAL B 156 64.384 22.006 154.252 1.00 21.61 B C ATOM 1667 CG1 VAL B 156 64.096 23.462 154.600 1.00 19.88 B C ATOM 1668 CG2 VAL B 156 63.158 21.135 154.537 1.00 20.58 B C ATOM 1669 C VAL B 156 64.951 20.447 152.345 1.00 23.15 B C ATOM 1670 O VAL B 156 64.240 19.988 151.456 1.00 23.36 B O ATOM 1671 N TYR B 157 65.864 19.717 152.982 1.00 24.51 B N ATOM 1672 CA TYR B 157 66.100 18.321 152.613 1.00 25.70 B C ATOM 1673 CB TYR B 157 67.475 18.190 151.956 1.00 23.43 B C ATOM 1674 OG TYR B 157 67.634 19.050 150.728 1.00 23.94 B C ATOM 1675 OD1 TYR B 157 67.800 20.430 150.837 1.00 22.81 B C ATOM 1676 CE1 TYR B 157 67.891 21.233 149.703 1.00 24.82 B C ATOM 1677 CD2 TYR B 157 67.567 18.492 149.451 1.00 24.09 B C ATOM 1678 CE2 TYR B 157 67.658 19.285 148.313 1.00 24.05 B C ATOM 1679 CZ TYR B 157 67.820 20.652 148.445 1.00 25.74 B C ATOM 1680 OH TYR B 157 67.919 21.438 147.319 1.00 32.12 B O ATOM 1681 C TYR B 157 65.991 17.297 153.735 1.00 27.77 B C ATOM 1682 O TYR B 157 66.644 16.254 153.696 1.00 28.36 B O ATOM 1683 N SER B 158 65.162 17.576 154.731 1.00 29.96 B N ATOM 1684 CA SER B 158 65.006 16.641 155.834 1.00 32.14 B C ATOM 1685 CE SER B 158 65.751 17.144 157.077 1.00 32.84 B C ATOM 1686 OG SER B 158 65.274 18.414 157.490 1.00 34.79 B O ATOM 1687 C SER B 158 63.549 16.412 156.178 1.00 33.22 B C ATOM 1688 O SER B 158 62.667 17.155 155.750 1.00 29.83 B O ATOM 1689 N ARG B 159 63.319 15.376 156.973 1.00 37.03 B N ATOM 1690 CA ARG B 159 61.990 14.999 157.418 1.00 40.29 B C ATOM 1691 CB ARG B 159 62.071 13.676 158.176 1.00 46.56 B C ATOM 1692 CC ARG B 159 60.957 12.699 157.863 1.00 57.91 B C ATOM 1693 CD ARG B 159 61.049 11.467 158.757 1.00 64.70 B C ATOM 1694 NE ARG B 159 59.974 10.514 158.490 1.00 70.47 B N ATOM 1695 CZ ARG B 159 59.694 9.466 159.260 1.00 73.51 B C ATOM 1696 NH1 ARG B 159 58.698 8.651 158.937 1.00 74.22 B N ATOM 1697 NH2 ARG B 159 60.406 9.237 160.357 1.00 74.50 B N ATOM 1698 C ARG B 159 61.395 16.078 158.325 1.00 38.61 B C ATOM 1699 O ARG B 159 60.264 15.949 158.781 1.00 39.20 B O ATOM 1700 N ASP B 160 62.160 17.135 158.583 1.00 37.90 B N ATOM 1701 CA ASP B 160 61.707 18.233 159.438 1.00 36.97 B C ATOM 1702 CB ASP B 160 62.894 19.043 159.971 1.00 42.42 B C ATOM 1703 CG ASP B 160 63.908 18.195 160.698 1.00 46.87 B C ATOM 1704 OD1 ASP B 160 63.505 17.346 161.523 1.00 49.44 B O ATOM 1705 OD2 ASP B 160 65.116 18.393 160.451 1.00 50.63 B O ATOM 1706 C ASP B 160 60.784 19.198 158.706 1.00 33.52 B C ATOM 1707 O ASP B 160 60.165 20.065 159.326 1.00 33.69 B O ATOM 1708 N ALA B 161 60.706 19.065 157.389 1.00 29.73 B N ATOM 1709 CA ALA B 161 59.864 19.948 156.594 1.00 25.02 B C ATOM 1710 CB ALA B 161 60.019 19.620 155.116 1.00 24.48 B C ATOM 1711 C ALA B 161 58.408 19.808 157.005 1.00 22.73 B C ATOM 1712 O ALA B 161 57.983 18.743 157.453 1.00 18.59 B O ATOM 1713 N ASP B 162 57.644 20.886 156.865 1.00 20.01 B N ATOM 1714 CA ASP B 162 56.226 20.835 157.207 1.00 19.49 B C ATOM 1715 CB ASP B 162 55.625 22.240 157.298 1.00 17.17 B C ATOM 1716 CG ASP B 162 56.279 23.087 158.365 1.00 15.31 B C ATOM 1717 OD1 ASP B 162 56.422 22.601 159.505 1.00 16.45 B O ATOM 1718 OD2 ASP B 162 56.643 24.242 158.066 1.00 14.81 B O ATOM 1719 C ASP B 162 55.486 20.055 156.128 1.00 20.86 B C ATOM 1720 O ASP B 162 54.620 19.240 156.417 1.00 19.12 B O ATOM 1721 N ILE B 163 55.836 20.312 154.875 1.00 20.30 B N ATOM 1722 CA ILE B 163 55.183 19.646 153.760 1.00 17.16 B C ATOM 1723 CB ILE B 163 54.640 20.692 152.748 1.00 19.96 B C ATOM 1724 CG2 ILE B 163 54.032 19.995 151.530 1.00 16.75 B C ATOM 1725 CG1 ILE B 163 53.611 21.587 153.449 1.00 20.77 B C ATOM 1726 CD1 ILE B 163 53.139 22.769 152.625 1.00 16.61 B C ATOM 1727 C ILE B 163 56.138 18.694 153.058 1.00 15.84 B C ATOM 1728 O ILE B 163 57.096 19.114 152.411 1.00 16.45 B O ATOM 1729 N VAL B 164 55.883 17.405 153.207 1.00 13.42 B N ATOM 1730 CA VAL B 164 56.711 16.408 152.567 1.00 13.63 B C ATOM 1731 CB VAL B 164 56.977 15.221 153.498 1.00 13.46 B C ATOM 1732 CG1 VAL B 164 57.737 14.136 152.750 1.00 11.25 B C ATOM 1733 CG2 VAL B 164 57.773 15.694 154.713 1.00 12.79 B C ATOM 1734 C VAL B 164 55.991 15.939 151.310 1.00 14.94 B C ATOM 1735 O VAL B 164 54.826 15.535 151.358 1.00 15.76 B O ATOM 1736 N ILE B 165 56.698 16.015 150.187 1.00 13.79 B N ATOM 1737 CA ILE B 165 56.165 15.636 148.886 1.00 12.71 B C ATOM 1738 CB ILE B 165 56.472 16.714 147.857 1.00 14.97 B C ATOM 1739 CG2 ILE B 165 55.912 16.306 146.503 1.00 13.61 B C ATOM 1740 CG1 ILE B 165 55.919 18.059 148.348 1.00 13.19 B C ATOM 1741 CD1 ILE B 165 56.377 19.259 147.543 1.00 14.12 B C ATOM 1742 C ILE B 165 56.749 14.334 148.381 1.00 13.67 B C ATOM 1743 O ILE B 165 57.949 14.096 148.491 1.00 11.91 B O ATOM 1744 N GLN B 166 55.903 13.481 147.820 1.00 14.64 B N ATOM 1745 CA GLN B 166 56.400 12.230 147.291 1.00 17.38 B C ATOM 1746 CB GLN B 166 56.599 11.209 148.412 1.00 20.52 B C ATOM 1747 CG GLN B 166 55.328 10.614 148.956 1.00 28.99 B C ATOM 1748 CD GLN B 166 55.589 9.395 149.828 1.00 34.11 B C ATOM 1749 OE1 GLN B 166 55.972 8.329 149.334 1.00 34.45 B O ATOM 1750 NE2 GLN B 166 55.392 9.550 151.134 1.00 36.00 B N ATOM 1751 C GLN B 166 55.511 11.625 146.226 1.00 16.18 B C ATOM 1752 O GLN B 166 54.304 11.856 146.204 1.00 14.81 B O ATOM 1753 N PHE B 167 56.141 10.859 145.339 1.00 14.40 B N ATOM 1754 CA PHE B 167 55.463 10.147 144.274 1.00 13.46 B C ATOM 1755 CB PHE B 167 56.237 10.257 142.959 1.00 9.79 B C ATOM 1756 CG PHE B 167 56.265 11.642 142.386 1.00 11.55 B C ATOM 1757 CD1 PHE B 167 57.172 12.581 142.852 1.00 12.24 B C ATOM 1758 CD2 PHE B 167 55.371 12.012 141.388 1.00 12.04 B C ATOM 1759 CE1 PHE B 167 57.191 13.874 142.334 1.00 12.05 B C ATOM 1760 CE2 PHE B 167 55.379 13.306 140.865 1.00 11.98 B C ATOM 1761 CZ PHE B 167 56.288 14.237 141.338 1.00 13.47 B C ATOM 1762 C PHE B 167 55.414 8.685 144.681 1.00 14.78 B C ATOM 1763 O PHE B 167 56.389 8.160 145.202 1.00 16.19 B O ATOM 1764 N GLY B 168 54.283 8.028 144.446 1.00 16.63 B N ATOM 1765 CA GLY B 168 54.170 6.626 144.795 1.00 18.19 B C ATOM 1766 C GLY B 168 53.143 5.900 143.951 1.00 20.06 B C ATOM 1767 O GLY B 168 52.352 6.535 143.260 1.00 21.45 B O ATOM 1768 N VAL B 169 53.168 4.572 143.988 1.00 21.07 B N ATOM 1769 CA VAL B 169 52.206 3.764 143.247 1.00 22.74 B C ATOM 1770 CB VAL B 169 52.875 2.967 142.109 1.00 22.64 B C ATOM 1771 CG1 VAL B 169 53.593 3.913 141.170 1.00 22.95 B C ATOM 1772 CG2 VAL B 169 53.832 1.943 142.686 1.00 23.18 B C ATOM 1773 C VAL B 169 51.547 2.773 144.203 1.00 24.58 B C ATOM 1774 O VAL B 169 52.210 2.174 145.055 1.00 24.53 B O ATOM 1775 N ALA B 170 50.238 2.607 144.061 1.00 25.72 B N ATOM 1776 CA ALA B 170 49.498 1.690 144.912 1.00 25.50 B C ATOM 1777 CB ALA B 170 49.845 0.256 144.543 1.00 24.40 B C ATOM 1778 C ALA B 170 49.826 1.959 146.379 1.00 25.00 B C ATOM 1779 O ALA B 170 49.761 3.106 146.836 1.00 23.10 B O ATOM 1780 N GLU B 171 50.179 0.902 147.105 1.00 26.18 B N ATOM 1781 CA GLU B 171 50.521 1.002 148.523 1.00 30.44 B C ATOM 1782 CB GLU B 171 50.756 −0.391 149.113 1.00 37.69 B C ATOM 1783 CG GLU B 171 49.929 −1.502 148.484 1.00 50.32 B C ATOM 1784 CD GLU B 171 48.452 −1.388 148.800 1.00 56.96 B C ATOM 1785 OE1 GLU B 171 47.671 −2.226 148.296 1.00 59.68 B O ATOM 1786 OE2 GLU B 171 48.074 −0.464 149.555 1.00 61.18 B O ATOM 1787 C GLU B 171 51.810 1.802 148.647 1.00 28.21 B C ATOM 1788 O GLU B 171 52.839 1.399 148.108 1.00 26.23 B O ATOM 1789 N HIS B 172 51.776 2.922 149.360 1.00 26.31 B N ATOM 1790 CA HIS B 172 52.989 3.723 149.488 1.00 26.29 B C ATOM 1791 CB HIS B 172 52.935 4.898 148.500 1.00 21.05 B C ATOM 1792 CG HIS B 172 51.733 5.777 148.671 1.00 19.27 B C ATOM 1793 CD2 HIS B 172 51.536 6.874 149.438 1.00 17.23 B C ATOM 1794 ND1 HIS B 172 50.526 5.519 148.056 1.00 15.56 B N ATOM 1795 CE1 HIS B 172 49.638 6.416 148.441 1.00 14.96 B C ATOM 1796 NE2 HIS B 172 50.225 7.248 149.281 1.00 13.17 B N ATOM 1797 C HIS B 172 53.334 4.246 150.890 1.00 27.55 B C ATOM 1798 O HIS B 172 54.057 5.231 151.019 1.00 26.45 B O ATOM 1799 N GLY B 173 52.831 3.601 151.940 1.00 30.22 B N ATOM 1800 CA GLY B 173 53.154 4.070 153.280 1.00 32.63 B C ATOM 1801 C GLY B 173 51.972 4.307 154.198 1.00 35.23 B C ATOM 1802 O GLY B 173 51.827 3.621 155.209 1.00 39.12 B O ATOM 1803 N ASP B 174 51.138 5.289 153.875 1.00 33.34 B N ATOM 1804 CA ASP B 174 49.968 5.563 154.692 1.00 33.01 B C ATOM 1805 CB ASP B 174 49.343 6.899 154.299 1.00 34.56 B C ATOM 1806 CG ASP B 174 49.366 7.138 152.797 1.00 33.72 B C ATOM 1807 OD1 ASP B 174 49.119 6.191 152.023 1.00 30.99 B O ATOM 1808 OD2 ASP B 174 49.623 8.286 152.395 1.00 32.06 B O ATOM 1809 C ASP B 174 48.969 4.438 154.475 1.00 33.84 B C ATOM 1810 O ASP B 174 49.323 3.368 153.982 1.00 35.39 B O ATOM 1811 N GLY B 175 47.719 4.666 154.837 1.00 34.25 B N ATOM 1812 CA GLY B 175 46.732 3.620 154.641 1.00 36.75 B C ATOM 1813 C GLY B 175 45.836 3.952 153.474 1.00 35.04 B C ATOM 1814 O GLY B 175 44.705 3.478 153.390 1.00 37.61 B O ATOM 1815 N TYR B 176 46.359 4.768 152.566 1.00 33.73 B N ATOM 1816 CA TYR B 176 45.597 5.200 151.409 1.00 32.53 B C ATOM 1817 CB TYR B 176 45.285 6.690 151.545 1.00 35.60 B C ATOM 1818 CG TYR B 176 44.636 7.044 152.867 1.00 40.89 B C ATOM 1819 CD1 TYR B 176 45.334 6.907 154.070 1.00 43.33 B C ATOM 1820 CE1 TYR B 176 44.736 7.204 155.290 1.00 43.67 B C ATOM 1821 CD2 TYR B 176 43.318 7.492 152.922 1.00 42.09 B C ATOM 1822 CE2 TYR B 176 42.711 7.794 154.140 1.00 42.63 B C ATOM 1823 CZ TYR B 176 43.426 7.647 155.317 1.00 43.63 B C ATOM 1824 OH TYR B 176 42.835 7.947 156.519 1.00 45.29 B O ATOM 1825 C TYR B 176 46.309 4.931 150.089 1.00 30.01 B C ATOM 1826 O TYR B 176 46.907 5.825 149.503 1.00 29.44 B O ATOM 1827 N PRO B 177 46.255 3.686 149.604 1.00 29.94 B N ATOM 1828 CD PRO B 177 45.706 2.475 150.238 1.00 28.60 B C ATOM 1829 CA PRO B 177 46.918 3.366 148.335 1.00 28.82 B C ATOM 1830 CB PRO B 177 46.838 1.843 148.280 1.00 29.21 B C ATOM 1831 CG PRO B 177 45.590 1.533 149.067 1.00 30.96 B C ATOM 1832 C PRO B 177 46.253 4.029 147.128 1.00 28.62 B C ATOM 1833 O PRO B 177 45.070 4.372 147.167 1.00 30.61 B O ATOM 1834 N PHE B 178 47.023 4.225 146.062 1.00 26.71 B N ATOM 1835 CA PHE B 178 46.475 4.825 144.851 1.00 26.70 B C ATOM 1836 CB PHE B 178 47.568 5.547 144.055 1.00 22.42 B C ATOM 1837 CG PHE B 178 48.019 6.842 144.687 1.00 17.95 B C ATOM 1838 CD1 PHE B 178 47.108 7.871 144.919 1.00 16.47 B C ATOM 1839 CD2 PHE B 178 49.349 7.029 145.058 1.00 17.30 B C ATOM 1840 CE1 PHE B 178 47.511 9.069 145.511 1.00 14.31 B C ATOM 1841 CE2 PHE B 178 49.765 8.221 145.650 1.00 14.81 B C ATOM 1842 CZ PHE B 178 48.842 9.245 145.877 1.00 16.31 B C ATOM 1843 C PHE B 178 45.810 3.733 144.017 1.00 26.77 B C ATOM 1844 O PHE B 178 46.020 2.546 144.261 1.00 23.82 B O ATOM 1845 N ASP B 179 45.017 4.142 143.032 1.00 28.61 B N ATOM 1846 CA ASP B 179 44.259 3.209 142.203 1.00 29.98 B C ATOM 1847 CS ASP B 179 42.808 3.674 142.164 1.00 29.97 B C ATOM 1848 CG ASP B 179 42.698 5.131 141.810 1.00 30.41 B C ATOM 1849 OD1 ASP B 179 43.709 5.661 141.331 1.00 35.31 B O ATOM 1850 OD2 ASP B 179 41.631 5.750 141.995 1.00 33.11 B O ATOM 1851 C ASP B 179 44.731 2.976 140.768 1.00 30.43 B C ATOM 1852 O ASP B 179 43.924 2.646 139.909 1.00 30.49 B O ATOM 1853 N GLY B 180 46.020 3.128 140.499 1.00 30.89 B N ATOM 1854 CA GLY B 180 46.493 2.905 139.146 1.00 29.05 B C ATOM 1855 C GLY B 180 46.142 4.064 138.237 1.00 29.44 B C ATOM 1856 O GLY B 180 45.789 5.131 138.723 1.00 25.58 B O ATOM 1857 N LYS B 181 46.217 3.849 136.925 1.00 29.06 B N ATOM 1858 CA LYS B 181 45.936 4.895 135.943 1.00 30.26 B C ATOM 1859 CB LYS B 181 46.100 4.322 134.535 1.00 33.27 B C ATOM 1860 CG LYS B 181 45.992 5.346 133.426 1.00 36.93 B C ATOM 1861 CD LYS B 181 46.258 4.704 132.077 1.00 41.28 B C ATOM 1862 CE LYS B 181 46.044 5.691 130.936 1.00 44.88 B C ATOM 1863 NZ LYS B 181 44.634 6.1761 30.859 1.00 43.95 B N ATOM 1864 C LYS B 181 44.565 5.565 136.087 1.00 28.94 B C ATOM 1865 O LYS B 181 43.545 4.901 136.239 1.00 30.47 B O ATOM 1866 N ASP B 182 44.561 6.892 136.034 1.00 29.99 B N ATOM 1867 CA ASP B 182 43.347 7.692 136.166 1.00 30.47 B C ATOM 1868 CB ASP B 182 42.367 7.376 135.035 1.00 35.39 B C ATOM 1869 CG ASP B 182 42.877 7.826 133.684 1.00 38.40 B C ATOM 1870 OD1 ASP B 182 43.081 9.045 133.491 1.00 39.28 B O ATOM 1871 OD2 ASP B 182 43.078 6.954 132.814 1.00 42.49 B O ATOM 1872 C ASP B 182 42.642 7.509 137.506 1.00 31.65 B C ATOM 1873 O ASP B 182 43.099 6.765 138.363 1.00 32.44 B O ATOM 1874 N GLY B 183 41.509 8.181 137.670 1.00 29.41 B N ATOM 1875 CA GLY B 183 40.774 8.091 138.912 1.00 27.84 B C ATOM 1876 C GLY B 183 41.335 9.123 139.864 1.00 27.88 B C ATOM 1877 O GLY B 183 41.355 10.310 139.549 1.00 29.24 B O ATOM 1878 N LEU B 184 41.792 8.678 141.030 1.00 27.15 B N ATOM 1879 CA LEU B 184 42.376 9.585 142.015 1.00 25.82 B C ATOM 1880 CB LEU B 184 42.493 8.878 143.359 1.00 27.95 B C ATOM 1881 CG LEU B 184 42.940 9.772 144.507 1.00 30.41 B C ATOM 1882 CD1 LEU B 184 41.855 10.797 144.779 1.00 28.19 B C ATOM 1883 CD2 LEU B 184 43.205 8.927 145.746 1.00 34.06 B C ATOM 1884 C LEU B 184 43.771 9.971 141.520 1.00 22.60 B C ATOM 1885 O LEU B 184 44.593 9.106 141.265 1.00 17.85 B O ATOM 1886 N LEU B 185 44.047 11.262 141.397 1.00 22.16 B N ATOM 1887 CA LEU B 185 45.346 11.700 140.884 1.00 22.33 B C ATOM 1888 CB LEU B 185 45.177 13.002 140.095 1.00 19.27 B C ATOM 1889 CG LEU B 185 44.127 12.970 138.979 1.00 20.81 B C ATOM 1890 CD1 LEU B 185 44.110 14.305 138.252 1.00 12.81 B C ATOM 1891 CD2 LEU B 185 44.425 11.823 138.013 1.00 17.71 B C ATOM 1892 C LEU B 185 46.400 11.897 141.965 1.00 23.14 B C ATOM 1893 O LEU B 185 47.593 11.658 141.749 1.00 22.98 B O ATOM 1894 N ALA B 186 45.948 12.331 143.131 1.00 23.03 B N ATOM 1895 CA ALA B 186 46.830 12.585 144.255 1.00 22.63 B C ATOM 1896 CB ALA B 186 47.717 13.768 143.942 1.00 21.82 B C ATOM 1897 C ALA B 186 45.974 12.896 145.472 1.00 23.10 B C ATOM 1898 O ALA B 186 44.751 12.932 145.378 1.00 25.16 B O ATOM 1899 N HIS B 187 46.622 13.104 146.613 1.00 22.01 B N ATOM 1900 CA HIS B 187 45.927 13.458 147.840 1.00 21.61 B C ATOM 1901 CB HIS B 187 45.218 12.237 148.451 1.00 19.44 B C ATOM 1902 CG HIS B 187 46.126 11.110 148.838 1.00 21.62 B C ATOM 1903 CD2 HIS B 187 47.343 11.101 149.434 1.00 23.01 B C ATOM 1904 ND1 HIS B 187 45.771 9.787 148.673 1.00 20.29 B N ATOM 1905 CE1 HIS B 187 46.730 9.013 149.151 1.00 20.79 B C ATOM 1906 NE2 HIS B 187 47.695 9.786 149.619 1.00 19.38 B N ATOM 1907 C HIS B 187 46.898 14.097 148.822 1.00 22.17 B C ATOM 1908 O HIS B 187 48.086 13.786 148.818 1.00 21.16 B O ATOM 1909 N ALA B 188 46.386 15.015 149.637 1.00 19.90 B N ATOM 1910 CA ALA B 188 47.191 15.727 150.615 1.00 21.04 B C ATOM 1911 CB ALA B 188 47.386 17.165 150.169 1.00 16.20 B C ATOM 1912 C ALA B 188 46.511 15.689 151.981 1.00 24.29 B C ATOM 1913 O ALA B 188 45.342 15.313 152.091 1.00 23.00 B O ATOM 1914 N PHE B 189 47.248 16.076 153.020 1.00 25.22 B N ATOM 1915 CA PHE B 189 46.712 16.081 154.373 1.00 23.69 B C ATOM 1916 CB PHE B 189 47.532 15.162 155.290 1.00 23.93 B C ATOM 1917 CG PHE B 189 47.565 13.731 154.839 1.00 26.85 B C ATOM 1918 CD1 PHE B 189 48.483 13.308 153.881 1.00 29.60 B C ATOM 1919 CD2 PHE B 189 46.668 12.806 155.358 1.00 27.63 B C ATOM 1920 CE1 PHE B 189 48.510 11.984 153.447 1.00 27.95 B C ATOM 1921 CE2 PHE B 189 46.685 11.480 154.930 1.00 29.13 B C ATOM 1922 CZ PHE B 189 47.609 11.069 153.972 1.00 29.53 B C ATOM 1923 C PHE B 189 46.712 17.491 154.932 1.00 24.15 B C ATOM 1924 O PHE B 189 47.600 18.286 154.632 1.00 23.64 B O ATOM 1925 N PRO B 190 45.703 17.818 155.761 1.00 25.45 B N ATOM 1926 CD PRO B 190 44.626 16.901 156.165 1.00 24.82 B C ATOM 1927 CA PRO B 190 45.535 19.135 156.399 1.00 23.84 B C ATOM 1928 CB PRO B 190 44.211 18.998 157.151 1.00 23.85 B C ATOM 1929 CG PRO B 190 43.517 17.859 156.470 1.00 27.72 B C ATOM 1930 C PRO B 190 46.693 19.452 157.355 1.00 24.12 B C ATOM 1931 O PRO B 190 47.364 18.544 157.851 1.00 24.59 B O ATOM 1932 N PRO B 191 46.929 20.745 157.633 1.00 23.67 B N ATOM 1933 CD PRO B 191 46.130 21.889 157.160 1.00 22.01 B C ATOM 1934 CA PRO B 191 48.005 21.193 158.527 1.00 24.52 B C ATOM 1935 CB PRO B 191 47.668 22.660 158.756 1.00 23.21 B C ATOM 1936 CG PRO B 191 47.036 23.056 157.463 1.00 23.95 B C ATOM 1937 C PRO B 191 48.077 20.402 159.834 1.00 26.78 B C ATOM 1938 O PRO B 191 47.054 19.982 160.374 1.00 27.80 B O ATOM 1939 N GLY B 192 49.294 20.207 160.334 1.00 26.68 B N ATOM 1940 CA GLY B 192 49.490 19.459 161.563 1.00 25.28 B C ATOM 1941 C GLY B 192 50.851 18.786 161.573 1.00 26.25 B C ATOM 1942 O GLY B 192 51.653 19.026 160.671 1.00 27.65 B O ATOM 1943 N PRO B 193 51.145 17.935 162.574 1.00 26.70 B N ATOM 1944 CD PRO B 193 50.356 17.760 163.808 1.00 23.89 B C ATOM 1945 CA PRO B 193 52.428 17.233 162.685 1.00 26.43 B C ATOM 1946 CB PRO B 193 52.572 17.049 164.189 1.00 26.13 B C ATOM 1947 CG PRO B 193 51.173 16.742 164.588 1.00 24.53 B C ATOM 1948 C PRO B 193 52.463 15.901 161.947 1.00 25.56 B C ATOM 1949 O PRO B 193 51.423 15.356 161.592 1.00 28.95 B O ATOM 1950 N GLY B 194 53.665 15.379 161.721 1.00 24.12 B N ATOM 1951 CA GLY B 194 53.803 14.100 161.046 1.00 22.38 B C ATOM 1952 C GLY B 194 53.338 14.098 159.605 1.00 23.14 B C ATOM 1953 O GLY B 194 53.602 15.036 158.868 1.00 21.24 B O ATOM 1954 N ILE B 195 52.633 13.048 159.202 1.00 24.37 B N ATOM 1955 CA ILE B 195 52.147 12.941 157.832 1.00 26.26 B C ATOM 1956 CB ILE B 195 51.440 11.590 157.613 1.00 27.60 B C ATOM 1957 CG2 ILE B 195 50.131 11.561 158.386 1.00 27.08 B C ATOM 1958 CG1 ILE B 195 51.200 11.365 156.119 1.00 29.76 B C ATOM 1959 CD1 ILE B 195 50.620 10.012 155.789 1.00 31.30 B C ATOM 1960 C ILE B 195 51.194 14.085 157.479 1.00 26.36 B C ATOM 1961 O ILE B 195 50.921 14.343 156.309 1.00 27.06 B O ATOM 1962 N GLN B 196 50.704 14.781 158.498 1.00 26.62 B N ATOM 1963 CA GLN B 196 49.790 15.901 158.298 1.00 26.46 B C ATOM 1964 CB GLN B 196 49.359 16.457 159.654 1.00 29.46 B C ATOM 1965 CG GLN B 196 47.864 16.383 159.914 1.00 38.14 B C ATOM 1966 CD GLN B 196 47.323 14.967 159.860 1.00 41.94 B C ATOM 1967 OE1 GLN B 196 46.116 14.751 159.940 1.00 44.27 B O ATOM 1968 NE2 GLN B 196 48.215 13.993 159.727 1.00 46.11 B N ATOM 1969 C GLN B 196 50.459 16.998 157.482 1.00 23.79 B C ATOM 1970 O GLN B 196 51.576 17.367 157.768 1.00 25.59 B O ATOM 1971 N GLY B 197 49.774 17.524 156.472 1.00 23.38 B N ATOM 1972 CA GLY B 197 50.364 18.568 155.650 1.00 18.35 B C ATOM 1973 C GLY B 197 51.149 18.047 154.450 1.00 20.05 B C ATOM 1974 O GLY B 197 51.606 18.835 153.619 1.00 21.28 B O ATOM 1975 N ASP B 198 51.308 16.727 154.354 1.00 18.69 B N ATOM 1976 CA ASP B 198 52.049 16.115 153.253 1.00 18.67 B C ATOM 1977 CB ASP B 198 52.557 14.730 153.668 1.00 17.24 B C ATOM 1978 CG ASP B 198 53.613 14.794 154.764 1.00 19.44 B C ATOM 1979 OD1 ASP B 198 53.978 15.912 155.160 1.00 14.37 B O ATOM 1980 OD2 ASP B 198 54.080 13.730 155.220 1.00 16.31 B O ATOM 1981 C ASP B 198 51.203 15.996 151.974 1.00 20.96 B C ATOM 1982 O ASP B 198 49.971 16.042 152.029 1.00 21.22 B O ATOM 1983 N ALA B 199 51.872 15.836 150.831 1.00 18.26 B N ATOM 1984 CA ALA B 199 51.197 15.722 149.536 1.00 17.33 B C ATOM 1985 CB ALA B 199 51.326 17.027 148.771 1.00 16.82 B C ATOM 1986 C ALA B 199 51.803 14.586 148.728 1.00 18.72 B C ATOM 1987 O ALA B 199 53.004 14.569 148.483 1.00 20.07 B O ATOM 1988 N HIS B 200 50.968 13.639 148.314 1.00 17.89 B N ATOM 1989 CA HIS B 200 51.424 12.481 147.555 1.00 15.98 B C ATOM 1990 CB HIS B 200 51.092 11.215 148.334 1.00 17.39 B C ATOM 1991 CG HIS B 200 51.623 11.212 149.736 1.00 20.36 B C ATOM 1992 CD2 HIS B 200 52.599 11.944 150.325 1.00 17.40 B C ATOM 1993 ND1 HIS B 200 51.160 10.349 150.704 1.00 18.51 B N ATOM 1994 CE1 HIS B 200 51.827 10.546 151.826 1.00 17.19 B C ATOM 1995 NB2 HIS B 200 52.706 11.508 151.623 1.00 17.14 B N ATOM 1996 C HIS B 200 50.786 12.427 146.168 1.00 18.64 B C ATOM 1997 O HIS B 200 49.591 12.668 146.016 1.00 18.44 B O ATOM 1998 N PHE B 201 51.594 12.105 145.160 1.00 19.00 B N ATOM 1999 CA PHE B 201 51.128 12.046 143.776 1.00 15.37 B C ATOM 2000 CB PHE B 201 51.929 13.027 142.912 1.00 16.11 B C ATOM 2001 CG PHE B 201 51.907 14.444 143.421 1.00 14.27 B C ATOM 2002 CD1 PHE B 201 52.747 14.840 144.459 1.00 15.41 B C ATOM 2003 CD2 PHE B 201 51.017 15.374 142.887 1.00 13.45 B C ATOM 2004 CE1 PHE B 201 52.704 16.143 144.961 1.00 15.16 B C ATOM 2005 CE2 PHE B 201 50.962 16.685 143.380 1.00 14.52 B C ATOM 2006 CZ PHE B 201 51.806 17.071 144.418 1.00 14.98 B C ATOM 2007 C PHE B 201 51.227 10.650 143.185 1.00 15.36 B C ATOM 2008 O PHE B 201 52.257 9.993 143.293 1.00 15.05 B O ATOM 2009 N ASP B 202 50.144 10.204 142.555 1.00 16.99 B N ATOM 2010 CA ASP B 202 50.094 8.877 141.941 1.00 18.47 B C ATOM 2011 CB ASP B 202 48.660 8.502 141.583 1.00 16.97 B C ATOM 2012 CG ASP B 202 48.546 7.080 141.116 1.00 17.69 B C ATOM 2013 OD1 ASP B 202 49.567 6.496 140.725 1.00 24.22 B O ATOM 2014 OD2 ASP B 202 47.442 6.530 141.132 1.00 22.67 B O ATOM 2015 C ASP B 202 50.944 8.843 140.673 1.00 17.99 B C ATOM 2016 O ASP B 202 50.604 9.460 139.670 1.00 16.40 B O ATOM 2017 N ASP B 203 52.039 8.101 140.722 1.00 18.18 B N ATOM 2018 CA ASP B 203 52.943 8.020 139.593 1.00 19.10 B C ATOM 2019 CB ASP B 203 54.360 7.745 140.098 1.00 18.63 B C ATOM 2020 CG ASP B 203 55.424 8.234 139.147 1.00 21.55 B C ATOM 2021 OD1 ASP B 203 55.153 9.165 138.359 1.00 22.68 B O ATOM 2022 OD2 ASP B 203 56.546 7.700 139.204 1.00 24.38 B O ATOM 2023 C ASP B 203 52.522 6.977 138.560 1.00 22.02 B C ATOM 2024 O ASP B 203 53.328 6.553 137.739 1.00 22.79 B O ATOM 2025 N ASP B 204 51.274 6.529 138.627 1.00 21.73 B N ATOM 2026 CA ASP B 204 50.772 5.589 137.631 1.00 20.62 B C ATOM 2027 CB ASP B 204 49.729 4.635 138.212 1.00 19.80 B C ATOM 2028 CG ASP B 204 50.304 3.270 138.551 1.00 22.45 B C ATOM 2029 OD1 ASP B 204 51.334 2.884 137.963 1.00 20.45 B O ATOM 2030 OD2 ASP B 204 49.709 2.571 139.399 1.00 23.05 B O ATOM 2031 C ASP B 204 50.123 6.478 136.570 1.00 20.79 B C ATOM 2032 O ASP B 204 49.739 6.016 135.504 1.00 23.31 B O ATOM 2033 N GLU B 205 50.008 7.763 136.890 1.00 18.69 B N ATOM 2034 CA GLU B 205 49.441 8.755 135.987 1.00 20.13 B C ATOM 2035 CB GLU B 205 48.874 9.931 136.778 1.00 20.83 B C ATOM 2036 CG GLU B 205 47.935 9.526 137.894 1.00 29.96 B C ATOM 2037 CD GLU B 205 46.627 8.986 137.377 1.00 33.57 B C ATOM 2038 OB1 GLU B 205 46.617 8.360 136.293 1.00 36.59 B O ATOM 2039 OE2 GLU B 205 45.607 9.185 138.060 1.00 40.04 B O ATOM 2040 C GLU B 205 50.560 9.285 135.099 1.00 21.01 B C ATOM 2041 O GLU B 205 51.725 9.238 135.477 1.00 19.13 B O ATOM 2042 N LEU B 206 50.207 9.795 133.924 1.00 18.61 B N ATOM 2043 CA LEU B 206 51.204 10.366 133.026 1.00 17.96 B C ATOM 2044 CB LEU B 206 50.758 10.242 131.568 1.00 18.74 B C ATOM 2045 CG LEU B 206 51.617 10.985 130.532 1.00 19.98 B C ATOM 2046 CD1 LEU B 206 53.062 10.519 130.627 1.00 18.61 B C ATOM 2047 CD2 LEU B 206 51.064 10.740 129.131 1.00 17.02 B C ATOM 2048 C LEU B 206 51.312 11.837 133.399 1.00 18.42 B C ATOM 2049 O LEU B 206 50.379 12.603 133.160 1.00 18.49 B O ATOM 2050 N TRP B 207 52.434 12.230 133.998 1.00 17.94 B N ATOM 2051 CA TRP B 207 52.618 13.622 134.401 1.00 16.68 B C ATOM 2052 CB TRP B 207 53.454 13.723 135.694 1.00 15.77 B C ATOM 2053 CG TRP B 207 52.752 13.143 136.870 1.00 14.61 B C ATOM 2054 CD2 TRP B 207 51.546 13.636 137.469 1.00 14.73 B C ATOM 2055 CE2 TRP B 207 51.165 12.708 138.464 1.00 14.79 B C ATOM 2056 CE3 TRP B 207 50.744 14.769 137.255 1.00 16.70 B C ATOM 2057 CD1 TRP B 207 53.051 11.979 137.511 1.00 13.93 B C ATOM 2058 NE1 TRP B 207 52.101 11.708 138.467 1.00 15.76 B N ATOM 2059 CZ2 TRP B 207 50.012 12.876 139.248 1.00 13.38 B C ATOM 2060 CZ3 TRP B 207 49.591 14.935 138.034 1.00 13.30 B C ATOM 2061 CH2 TRP B 207 49.241 13.990 139.016 1.00 13.83 B C ATOM 2062 C TRP B 207 53.267 14.435 133.299 1.00 16.25 B C ATOM 2063 O TRP B 207 54.230 14.003 132.665 1.00 14.91 B O ATOM 2064 N SER B 208 52.731 15.630 133.092 1.00 16.82 B N ATOM 2065 CA SER B 208 53.218 16.521 132.061 1.00 15.97 B C ATOM 2066 CB SER B 208 52.497 16.187 130.747 1.00 16.80 B C ATOM 2067 OG SER B 208 53.111 16.799 129.634 1.00 12.64 B O ATOM 2068 C SER B 208 52.924 17.953 132.496 1.00 17.15 B C ATOM 2069 O SER B 208 52.677 18.207 133.676 1.00 20.26 B O ATOM 2070 N LEU B 209 52.954 18.881 131.543 1.00 15.88 B N ATOM 2071 CA LEU B 209 52.680 20.294 131.800 1.00 15.39 B C ATOM 2072 CB LEU B 209 53.972 21.049 132.105 1.00 12.60 B C ATOM 2073 CG LEU B 209 54.744 20.758 133.401 1.00 16.29 B C ATOM 2074 CD1 LEU B 209 56.029 21.560 133.386 1.00 12.54 B C ATOM 2075 CD2 LEU B 209 53.904 21.118 134.638 1.00 12.78 B C ATOM 2076 C LEU B 209 52.044 20.901 130.558 1.00 16.86 B C ATOM 2077 O LEU B 209 52.335 20.471 129.453 1.00 16.65 B O ATOM 2078 N GLY B 210 51.181 21.898 130.739 1.00 20.56 B N ATOM 2079 CA GLY B 210 50.545 22.557 129.602 1.00 20.23 B C ATOM 2080 C GLY B 210 49.475 21.767 128.864 1.00 21.25 B C ATOM 2081 O GLY B 210 48.885 20.835 129.409 1.00 21.72 B O ATOM 2082 N LYS B 211 49.207 22.158 127.621 1.00 20.99 B N ATOM 2083 CA LYS B 211 48.217 21.473 126.795 1.00 21.58 B C ATOM 2084 CB LYS B 211 47.879 22.314 125.560 1.00 22.10 B C ATOM 2085 CG LYS B 211 47.094 23.564 125.878 1.00 24.12 B C ATOM 2086 CD LYS B 211 46.828 24.410 124.647 1.00 27.19 B C ATOM 2087 CE LYS B 211 48.099 25.058 124.149 1.00 30.98 B C ATOM 2088 NZ LYS B 211 47.812 26.127 123.147 1.00 36.83 B N ATOM 2089 C LYS B 211 48.804 20.142 126.355 1.00 22.13 B C ATOM 2090 O LYS B 211 50.029 19.997 126.286 1.00 23.20 B O ATOM 2091 N GLY B 212 47.940 19.180 126.044 1.00 18.79 B N ATOM 2092 CA GLY B 212 48.420 17.877 125.623 1.00 17.78 B C ATOM 2093 C GLY B 212 47.925 16.758 126.521 1.00 18.87 B C ATOM 2094 O GLY B 212 47.238 17.010 127.515 1.00 19.58 B O ATOM 2095 N GLN B 391 48.268 15.519 126.181 1.00 19.71 B N ATOM 2096 CA GLN B 391 47.828 14.384 126.978 1.00 24.27 B C ATOM 2097 CB GLN B 391 48.024 13.073 126.200 1.00 26.88 B C ATOM 2098 CG GLN B 391 49.371 12.436 126.354 1.00 36.19 B C ATOM 2099 CD GLN B 391 50.489 13.421 126.157 1.00 42.59 B C ATOM 2100 OE1 GLN B 391 50.568 14.090 125.131 1.00 51.17 B O ATOM 2101 NE2 GLN B 391 51.368 13.520 127.144 1.00 50.82 B N ATOM 2102 C GLN B 391 48.582 14.369 128.311 1.00 22.67 B C ATOM 2103 O GLN B 391 49.614 15.024 128.456 1.00 19.97 B O ATOM 2104 N GLY B 392 48.050 13.635 129.284 1.00 22.31 B N ATOM 2105 CA GLY B 392 48.672 13.586 130.592 1.00 20.72 B C ATOM 2106 C GLY B 392 48.050 14.651 131.473 1.00 19.93 B C ATOM 2107 O GLY B 392 47.238 15.452 131.010 1.00 20.51 B O ATOM 2108 N TYR B 393 48.433 14.672 132.744 1.00 20.46 B N ATOM 2109 CA TYR B 393 47.896 15.643 133.692 1.00 18.29 B C ATOM 2110 CB TYR B 393 47.421 14.924 134.962 1.00 20.08 B C ATOM 2111 CG TYR B 393 46.248 13.989 134.746 1.00 16.50 B C ATOM 2112 CD1 TYR B 393 44.957 14.490 134.602 1.00 17.97 B C ATOM 2113 CE1 TYR B 393 43.871 13.647 134.397 1.00 16.85 B C ATOM 2114 CD2 TYR B 393 46.429 12.610 134.675 1.00 18.06 B C ATOM 2115 CE2 TYR B 393 45.342 11.747 134.467 1.00 17.10 B C ATOM 2116 CZ TYR B 393 44.064 12.281 134.329 1.00 18.56 B C ATOM 2117 OH TYR B 393 42.974 11.463 134.100 1.00 18.94 B O ATOM 2118 C TYR B 393 48.964 16.653 134.050 1.00 17.76 B C ATOM 2119 O TYR B 393 50.138 16.304 134.130 1.00 22.05 B O ATOM 2120 N SER B 394 48.560 17.901 134.271 1.00 17.69 B N ATOM 2121 CA SER B 394 49.505 18.955 134.627 1.00 18.43 B C ATOM 2122 CB SER B 394 48.864 20.331 134.464 1.00 15.87 B C ATOM 2123 OG SER B 394 49.799 21.357 134.756 1.00 17.63 B O ATOM 2124 C SER B 394 49.974 18.806 136.066 1.00 19.32 B C ATOM 2125 O SER B 394 49.185 18.953 136.997 1.00 23.73 B O ATOM 2126 N LEU B 395 51.253 18.512 136.255 1.00 18.56 B N ATOM 2127 CA LEU B 395 51.785 18.373 137.604 1.00 17.72 B C ATOM 2128 CB LEU B 395 53.265 17.972 137.556 1.00 16.48 B C ATOM 2129 CG LEU B 395 53.993 17.751 138.889 1.00 15.25 B C ATOM 2130 CD1 LEU B 395 53.311 16.631 139.670 1.00 13.74 B C ATOM 2131 CD2 LEU B 395 55.457 17.409 138.628 1.00 10.40 B C ATOM 2132 C LEU B 395 51.624 19.710 138.329 1.00 18.62 B C ATOM 2133 O LEU B 395 51.285 19.746 139.507 1.00 19.25 B O ATOM 2134 N PHE B 396 51.853 20.803 137.605 1.00 16.65 B N ATOM 2135 CA PHE B 396 51.741 22.152 138.152 1.00 17.42 B C ATOM 2136 CB PHE B 396 52.035 23.181 137.057 1.00 16.61 B C ATOM 2137 CG PHE B 396 51.661 24.592 137.421 1.00 17.86 B C ATOM 2138 CD1 PHE B 396 52.306 25.261 138.456 1.00 17.66 B C ATOM 2139 CD2 PHE B 396 50.666 25.259 136.714 1.00 19.99 B C ATOM 2140 CE1 PHE B 396 51.966 26.580 138.782 1.00 17.56 B C ATOM 2141 CE2 PHE B 396 50.319 26.573 137.030 1.00 20.09 B C ATOM 2142 CZ PHE B 396 50.974 27.236 138.070 1.00 19.48 B C ATOM 2143 C PHE B 396 50.369 22.429 138.749 1.00 20.69 B C ATOM 2144 O PHE B 396 50.257 22.821 139.916 1.00 20.46 B O ATOM 2145 N LEU B 397 49.329 22.234 137.942 1.00 20.63 B N ATOM 2146 CA LEU B 397 47.958 22.472 138.381 1.00 19.67 B C ATOM 2147 CB LEU B 397 46.985 22.340 137.201 1.00 19.64 B C ATOM 2148 CG LEU B 397 47.038 23.424 136.122 1.00 18.58 B C ATOM 2149 CD1 LEU B 397 −45.965 23.156 135.086 1.00 15.91 B C ATOM 2150 CD2 LEU B 397 46.843 24.793 136.748 1.00 18.23 B C ATOM 2151 C LEU B 397 47.512 21.550 139.510 1.00 18.44 B C ATOM 2152 O LEU B 397 46.858 21.997 140.452 1.00 19.34 B O ATOM 2153 N VAL B 398 47.846 20.266 139.417 1.00 17.99 B N ATOM 2154 CA VAL B 398 47.464 19.326 140.466 1.00 19.04 B C ATOM 2155 CB VAL B 398 47.733 17.866 140.043 1.00 19.35 B C ATOM 2156 CG1 VAL B 398 47.353 16.905 141.173 1.00 15.55 B C ATOM 2157 CG2 VAL B 398 46.913 17.538 138.809 1.00 19.62 B C ATOM 2158 C VAL B 398 48.211 19.629 141.773 1.00 20.64 B C ATOM 2159 O VAL B 398 47.659 19.469 142.862 1.00 21.46 B O ATOM 2160 N ALA B 399 49.457 20.079 141.660 1.00 18.80 B N ATOM 2161 CA ALA B 399 50.254 20.411 142.834 1.00 21.04 B C ATOM 2162 CB ALA B 399 51.701 20.743 142.421 1.00 17.73 B C ATOM 2163 C ALA B 399 49.636 21.599 143.566 1.00 21.74 B C ATOM 2164 O ALA B 399 49.548 21.615 144.795 1.00 22.28 B O ATOM 2165 N ALA B 400 49.210 22.597 142.802 1.00 21.01 B N ATOM 2166 CA ALA B 400 48.611 23.787 143.378 1.00 20.55 B C ATOM 2167 CB ALA B 400 48.270 24.788 142.274 1.00 19.74 B C ATOM 2168 C ALA B 400 47.363 23.413 144.168 1.00 22.57 B C ATOM 2169 O ALA B 400 47.090 23.992 145.220 1.00 23.97 B O ATOM 2170 N HIS B 401 46.612 22.442 143.658 1.00 22.90 B N ATOM 2171 CA HIS B 401 45.397 21.980 144.321 1.00 23.48 B C ATOM 2172 CB HIS B 401 44.616 21.041 143.395 1.00 22.18 B C ATOM 2173 CG HIS B 401 43.328 20.544 143.976 1.00 23.80 B C ATOM 2174 CD2 HIS B 401 43.044 19.429 144.691 1.00 21.37 B C ATOM 2175 ND1 HIS B 401 42.138 21.230 143.847 1.00 23.81 B N ATOM 2176 CE1 HIS B 401 41.177 20.557 144.454 1.00 24.18 B C ATOM 2177 NE2 HIS B 401 41.699 19.461 144.976 1.00 21.29 B N ATOM 2178 C HIS B 401 45.763 21.246 145.615 1.00 24.30 B C ATOM 2179 O HIS B 401 45.192 21.519 146.673 1.00 24.53 B O ATOM 2180 N GLU B 402 46.714 20.317 145.529 1.00 23.82 B N ATOM 2181 CA GLU B 402 47.150 19.566 146.708 1.00 22.77 B C ATOM 2182 CB GLU B 402 48.217 18.530 146.341 1.00 22.35 B C ATOM 2183 CG GLU B 402 47.744 17.435 145.406 1.00 21.55 B C ATOM 2184 CD GLU B 402 46.298 17.071 145.636 1.00 21.21 B C ATOM 2185 OE1 GLU B 402 45.914 16.813 146.790 1.00 23.03 B O ATOM 2186 OE2 GLU B 402 45.539 17.043 144.654 1.00 26.51 B O ATOM 2187 C GLU B 402 47.710 20.486 147.785 1.00 22.14 B C ATOM 2188 O GLU B 402 47.431 20.301 148.966 1.00 24.45 B O ATOM 2189 N PHE B 403 48.504 21.473 147.382 1.00 22.87 B N ATOM 2190 CA PHE B 403 49.079 22.396 148.348 1.00 23.58 B C ATOM 2191 CB PHE B 403 50.124 23.308 147.688 1.00 20.83 B C ATOM 2192 CG PHE B 403 51.322 22.571 147.140 1.00 22.36 B C ATOM 2193 CD1 PHE B 403 51.587 21.252 147.518 1.00 20.84 B C ATOM 2194 CD2 PHE B 403 52.175 23.189 146.230 1.00 18.11 B C ATOM 2195 CE1 PHE B 403 52.682 20.560 146.989 1.00 21.54 B C ATOM 2196 CE2 PHE B 403 53.272 22.507 145.695 1.00 18.09 B C ATOM 2197 CZ PHE B 403 53.525 21.193 146.072 1.00 19.86 B C ATOM 2198 C PHE B 403 47.975 23.229 148.981 1.00 25.40 B C ATOM 2199 O PHE B 403 48.155 23.801 150.055 1.00 27.88 B O ATOM 2200 N GLY B 404 46.829 23.288 148.310 1.00 25.83 B N ATOM 2201 CA GLY B 404 45.703 24.038 148.833 1.00 25.16 B C ATOM 2202 C GLY B 404 45.208 23.328 150.076 1.00 25.03 B C ATOM 2203 O GLY B 404 44.922 23.953 151.096 1.00 24.69 B O ATOM 2204 N HIS B 405 45.110 22.008 149.980 1.00 23.03 B N ATOM 2205 CA HIS B 405 44.689 21.186 151.102 1.00 23.37 B C ATOM 2206 CB HIS B 405 44.537 19.731 150.668 1.00 21.33 B C ATOM 2207 CG HIS B 405 43.325 19.474 149.834 1.00 26.14 B C ATOM 2208 CD2 HIS B 405 43.164 18.781 148.683 1.00 23.33 B C ATOM 2209 ND1 HIS B 405 42.076 19.944 150.178 1.00 25.46 B N ATOM 2210 CE1 HIS B 405 41.198 19.551 149.274 1.00 26.71 B C ATOM 2211 NE2 HIS B 405 41.833 18.844 148.357 1.00 25.66 B N ATOM 2212 C HIS B 405 45.736 21.262 152.215 1.00 26.13 B C ATOM 2213 O HIS B 405 45.407 21.507 153.371 1.00 27.66 B O ATOM 2214 N ALA B 406 46.998 21.053 151.850 1.00 24.97 B N ATOM 2215 CA ALA B 406 48.099 21.082 152.802 1.00 25.23 B C ATOM 2216 CB ALA B 406 49.424 20.868 152.075 1.00 25.56 B C ATOM 2217 C ALA B 406 48.150 22.374 153.606 1.00 24.96 B C ATOM 2218 O ALA B 406 48.822 22.433 154.634 1.00 24.90 B O ATOM 2219 N LEU B 407 47.450 23.407 153.139 1.00 25.75 B N ATOM 2220 CA LEU B 407 47.424 24.683 153.849 1.00 26.02 B C ATOM 2221 CB LEU B 407 47.613 25.856 152.887 1.00 24.31 B C ATOM 2222 CG LEU B 407 48.951 25.959 152.146 1.00 27.21 B C ATOM 2223 CD1 LEU B 407 48.960 27.227 151.301 1.00 24.05 B C ATOM 2224 CD2 LEU B 407 50.110 25.979 153.132 1.00 25.82 B C ATOM 2225 C LEU B 407 46.121 24.869 154.627 1.00 27.45 B C ATOM 2226 O LEU B 407 45.947 25.868 155.323 1.00 28.27 B O ATOM 2227 N GLY B 408 45.208 23.910 154.504 1.00 27.89 B N ATOM 2228 CA GLY B 408 43.957 23.998 155.234 1.00 30.11 B C ATOM 2229 C GLY B 408 42.673 24.146 154.437 1.00 31.82 B C ATOM 2230 O GLY B 408 41.588 23.994 154.989 1.00 34.34 B O ATOM 2231 N LEU B 409 42.772 24.438 153.147 1.00 33.15 B N ATOM 2232 CA LEU B 409 41.575 24.601 152.325 1.00 32.57 B C ATOM 2233 CB LEU B 409 41.925 25.260 150.991 1.00 31.21 B C ATOM 2234 CG LEU B 409 42.400 26.711 151.009 1.00 32.82 B C ATOM 2235 CD1 LEU B 409 42.551 27.189 149.581 1.00 31.72 B C ATOM 2236 CD2 LEU B 409 41.397 27.589 151.747 1.00 33.90 B C ATOM 2237 C LEU B 409 40.826 23.305 152.034 1.00 33.31 B C ATOM 2238 O LEU B 409 41.427 22.250 151.850 1.00 32.51 B O ATOM 2239 N ASP B 410 39.500 23.396 152.003 1.00 35.18 B N ATOM 2240 CA ASP B 410 38.660 22.248 151.684 1.00 35.77 B C ATOM 2241 CB ASP B 410 37.422 22.186 152.595 1.00 42.82 B C ATOM 2242 CG ASP B 410 37.767 21.848 154.046 1.00 51.30 B C ATOM 2243 OD1 ASP B 410 38.706 21.050 154.273 1.00 53.65 B O ATOM 2244 OD2 ASP B 410 37.084 22.365 154.963 1.00 54.35 B O ATOM 2245 C ASP B 410 38.213 22.438 150.232 1.00 34.97 B C ATOM 2246 O ASP B 410 38.553 23.442 149.592 1.00 31.85 B O ATOM 2247 N HIS B 411 37.4522 1.482 149.713 1.00 32.49 B N ATOM 2248 CA HIS B 411 36.967 21.565 148.342 1.00 33.78 B C ATOM 2249 CB HIS B 411 36.312 20.248 147.944 1.00 30.30 B C ATOM 2250 CG HIS B 411 37.294 19.186 147.573 1.00 29.54 B C ATOM 2251 CD2 HIS B 411 38.532 19.270 147.036 1.00 27.76 B C ATOM 2252 ND1 HIS B 411 37.039 17.843 147.741 1.00 28.79 B N ATOM 2253 CE1 HIS B 411 38.079 17.144 147.325 1.00 28.07 B C ATOM 2254 NE2 HIS B 411 38.998 17.986 146.892 1.00 31.97 B N ATOM 2255 C HIS B 411 35.985 22.704 148.128 1.00 35.95 B C ATOM 2256 O HIS B 411 35.224 23.062 149.028 1.00 38.94 B O ATOM 2257 N SER B 412 36.013 23.274 146.927 1.00 37.78 B N ATOM 2258 CA SER B 412 35.115 24.365 146.566 1.00 38.30 B C ATOM 2259 CB SER B 412 35.846 25.417 145.726 1.00 37.72 B C ATOM 2260 OG SER B 412 34.953 26.426 145.281 1.00 34.94 B O ATOM 2261 C SER B 412 33.957 23.800 145.763 1.00 39.44 B C ATOM 2262 O SER B 412 34.050 22.703 145.213 1.00 38.62 B O ATOM 2263 N SER B 413 32.862 24.553 145.715 1.00 41.65 B N ATOM 2264 CA SER B 413 31.672 24.149 144.973 1.00 43.35 B C ATOM 2265 CB SER B 413 30.414 24.431 145.806 1.00 43.75 B C ATOM 2266 OG SER B 413 30.416 25.759 146.311 1.00 45.44 B O ATOM 2267 C SER B 413 31.620 24.910 143.644 1.00 43.39 B C ATOM 2268 O SER B 413 30.789 24.627 142.782 1.00 43.76 B O ATOM 2269 N VAL B 414 32.520 25.878 143.495 1.00 43.36 B N ATOM 2270 CA VAL B 414 32.613 26.679 142.282 1.00 45.01 B C ATOM 2271 CB VAL B 414 33.330 28.015 142.569 1.00 43.92 B C ATOM 2272 CG1 VAL B 414 33.395 28.862 141.307 1.00 42.90 B C ATOM 2273 CG2 VAL B 414 32.606 28.761 143.691 1.00 42.04 B C ATOM 2274 C VAL B 414 33.418 25.873 141.257 1.00 49.61 B C ATOM 2275 O VAL B 414 34.639 25.731 141.384 1.00 50.35 B O ATOM 2276 N PRO B 415 32.739 25.326 140.231 1.00 53.34 B N ATOM 2277 CD PRO B 415 31.281 25.415 140.033 1.00 54.43 B C ATOM 2278 CA PRO B 415 33.348 24.518 139.166 1.00 54.30 B C ATOM 2279 CB PRO B 415 32.200 24.343 138.173 1.00 56.11 B C ATOM 2280 CG PRO B 415 31.014 24.261 139.078 1.00 55.46 B C ATOM 2281 C PRO B 415 34.614 25.060 138.505 1.00 52.96 B C ATOM 2282 O PRO B 415 35.396 24.287 137.955 1.00 54.37 B O ATOM 2283 N GLU B 416 34.818 26.373 138.544 1.00 50.37 B N ATOM 2284 CA GLU B 416 36.016 26.946 137.940 1.00 48.82 B C ATOM 2285 CB GLU B 416 35.662 28.135 137.041 1.00 53.26 B C ATOM 2286 CG GLU B 416 34.714 29.151 137.651 1.00 58.55 B C ATOM 2287 CD GLU B 416 33.266 28.900 137.270 1.00 61.82 B C ATOM 2288 OE1 GLU B 416 32.399 29.699 137.684 1.00 62.91 B O ATOM 2289 OE2 GLU B 416 32.994 27.907 136.556 1.00 63.31 B O ATOM 2290 C GLU B 416 37.059 27.369 138.971 1.00 45.83 B C ATOM 2291 O GLU B 416 3 8.023 28.060 138.646 1.00 45.77 B O ATOM 2292 N ALA B 417 36.859 26.964 140.220 1.00 40.82 B N ATOM 2293 CA ALA B 417 37.811 27.283 141.278 1.00 37.74 B C ATOM 2294 CB ALA B 417 37.105 27.337 142.632 1.00 33.86 B C ATOM 2295 C ALA B 417 38.867 26.181 141.281 1.00 36.14 B C ATOM 2296 O ALA B 417 38.561 25.018 140.984 1.00 34.99 B O ATOM 2297 N LEU B 418 40.107 26.543 141.605 1.00 34.03 B N ATOM 2298 CA LEU B 418 41.191 25.569 141.648 1.00 30.71 B C ATOM 2299 CB LEU B 418 42.502 26.248 142.048 1.00 31.54 B C ATOM 2300 CG LEU B 418 43.718 25.338 142.279 1.00 30.96 B C ATOM 2301 CD1 LEU B 418 44.048 24.554 141.013 1.00 28.41 B C ATOM 2302 CD2 LEU B 418 44.908 26.190 142.704 1.00 29.00 B C ATOM 2303 C LEU B 418 40.886 24.445 142.629 1.00 30.37 B C ATOM 2304 O LEU B 418 41.261 23.295 142.402 1.00 31.03 B O ATOM 2305 N MET B 419 40.197 24.772 143.719 1.00 29.50 B N ATOM 2306 CA MET B 419 39.871 23.764 144.717 1.00 30.42 B C ATOM 2307 CB MET B 419 39.657 24.418 146.085 1.00 31.33 B C ATOM 2308 CG MET B 419 40.933 24.997 146.691 1.00 31.92 B C ATOM 2309 SD MET B 419 42.360 23.881 146.543 1.00 33.33 B S ATOM 2310 CE MET B 419 41.836 22.484 147.532 1.00 27.72 B C ATOM 2311 C MET B 419 38.688 22.862 144.381 1.00 30.21 B C ATOM 2312 O MET B 419 38.301 22.021 145.193 1.00 30.07 B O ATOM 2313 N TYR B 420 38.119 23.026 143.190 1.00 31.40 B N ATOM 2314 CA TYR B 420 37.006 22.180 142.769 1.00 31.95 B C ATOM 2315 CB TYR B 420 36.550 22.570 141.356 1.00 36.57 B C ATOM 2316 CG TYR B 420 35.227 21.951 140.953 1.00 41.51 B C ATOM 2317 CD1 TYR B 420 34.035 22.330 141.577 1.00 43.15 B C ATOM 2318 CE1 TYR B 420 32.824 21.719 141.250 1.00 43.91 B C ATOM 2319 CD2 TYR B 420 35.173 20.947 139.986 1.00 42.71 B C ATOM 2320 CE2 TYR B 420 33.971 20.330 139.655 1.00 43.77 B C ATOM 2321 CZ TYR B 420 32.803 20.717 140.290 1.00 44.73 B C ATOM 2322 OH TYR B 420 31.628 20.080 139.969 1.00 45.83 B O ATOM 2323 C TYR B 420 37.558 20.749 142.790 1.00 31.80 B C ATOM 2324 O TYR B 420 38.658 20.498 142.310 1.00 35.03 B O ATOM 2325 N PRO B 421 36.797 19.792 143.340 1.00 31.81 B N ATOM 2326 CD PRO B 421 35.430 20.002 143.846 1.00 31.47 B C ATOM 2327 CA PRO B 421 37.177 18.376 143.455 1.00 31.76 B C ATOM 2328 CB PRO B 421 36.033 17.783 144.277 1.00 32.37 B C ATOM 2329 CG PRO B 421 34.869 18.597 143.833 1.00 31.84 B C ATOM 2330 C PRO B 421 37.462 17.536 142.212 1.00 32.82 B C ATOM 2331 O PRO B 421 37.890 16.383 142.329 1.00 33.44 B O ATOM 2332 N MET B 422 37.225 18.078 141.028 1.00 34.03 B N ATOM 2333 CA MET B 422 37.469 17.303 139.819 1.00 34.21 B C ATOM 2334 CB MET B 422 36.156 17.127 139.050 1.00 40.49 B C ATOM 2335 CG MET B 422 35.093 16.379 139.863 1.00 46.52 B C ATOM 2336 SD MET B 422 33.548 16.039 138.978 1.00 54.83 B S ATOM 2337 CE MET B 422 33.899 14.421 138.287 1.00 48.46 B C ATOM 2338 C MET B 422 38.520 17.987 138.965 1.00 30.07 B C ATOM 2339 O MET B 422 38.610 19.208 138.960 1.00 27.30 B O ATOM 2340 N TYR B 423 39.328 17.205 138.256 1.00 30.57 B N ATOM 2341 CA TYR B 423 40.386 17.789 137.423 1.00 30.47 B C ATOM 2342 CB TYR B 423 41.432 16.730 137.066 1.00 28.25 B C ATOM 2343 CG TYR B 423 42.541 17.261 136.179 1.00 28.83 B C ATOM 2344 CD1 TYR B 423 43.549 18.077 136.695 1.00 26.05 B C ATOM 2345 CE1 TYR B 423 44.547 18.607 135.866 1.00 26.97 B C ATOM 2346 CD2 TYR B 423 42.557 16.984 134.809 1.00 29.17 B C ATOM 2347 CE2 TYR B 423 43.548 17.509 133.973 1.00 28.79 B C ATOM 2348 CZ TYR B 423 44.537 18.319 134.508 1.00 27.46 B C ATOM 2349 OH TYR B 423 45.499 18.848 133.679 1.00 29.00 B O ATOM 2350 C TYR B 423 39.891 18.450 136.132 1.00 29.81 B C ATOM 2351 O TYR B 423 38.997 17.941 135.456 1.00 28.16 B O ATOM 2352 N ALA B 424 40.496 19.583 135.795 1.00 30.84 B N ATOM 2353 CA ALA B 424 40.155 20.320 134.582 1.00 30.74 B C ATOM 2354 CB ALA B 424 38.891 21.137 134.809 1.00 30.80 B C ATOM 2355 C ALA B 424 41.316 21.241 134.201 1.00 31.98 B C ATOM 2356 O ALA B 424 41.662 22.147 134.960 1.00 30.87 B O ATOM 2357 N PHE B 425 41.916 21.016 133.030 1.00 32.65 B N ATOM 2358 CA PHE B 425 43.037 21.847 132.587 1.00 32.21 B C ATOM 2359 CB PHE B 425 43.761 21.219 131.387 1.00 29.42 B C ATOM 2360 CG PHE B 425 44.871 22.085 130.837 1.00 28.07 B C ATOM 2361 CD1 PHE B 425 44.635 22.967 129.783 1.00 26.46 B C ATOM 2362 CD2 PHE B 425 46.130 22.075 131.427 1.00 26.10 B C ATOM 2363 CE1 PHE B 425 45.636 23.828 129.334 1.00 26.71 B C ATOM 2364 CE2 PHE B 425 47.138 22.933 130.986 1.00 23.65 B C ATOM 2365 CZ PHE B 425 46.890 23.811 129.941 1.00 24.65 B C ATOM 2366 C PHE B 425 42.612 23.261 132.226 1.00 32.08 B C ATOM 2367 O PHE B 425 41.517 23.474 131.723 1.00 35.15 B 0 ATOM 2368 N THR B 426 43.489 24.226 132.480 1.00 32.53 B N ATOM 2369 CA THR B 426 43.193 25.618 132.170 1.00 31.99 B C ATOM 2370 CB THR B 426 42.377 26.297 133.309 1.00 33.76 B C ATOM 2371 OG1 THR B 426 42.153 27.674 132.979 1.00 35.23 B O ATOM 2372 CG2 THR B 426 43.132 26.236 134.638 1.00 32.87 B C ATOM 2373 C THR B 426 44.470 26.415 131.960 1.00 32.40 B ATOM 2374 O THR B 426 45.515 26.082 132.515 1.00 31.41 B O ATOM 2375 N GLU B 427 44.376 27.458 131.143 1.00 32.69 B N ATOM 2376 CA GLU B 427 45.505 28.338 130.877 1.00 34.12 B C ATOM 2377 CB GLU B 427 45.593 28.670 129.384 1.00 36.51 B C ATOM 2378 CG GLU B 427 45.967 27.493 128.490 1.00 41.69 B C ATOM 2379 CD GLU B 427 46.103 27.888 127.024 1.00 45.50 B C ATOM 2380 OE1 GLU B 427 45.082 28.269 126.410 1.00 44.55 B O ATOM 2381 OE2 GLU B 427 47.235 27.822 126.488 1.00 47.29 B O ATOM 2382 C GLU B 427 45.237 29.605 131.680 1.00 33.67 B C ATOM 2383 O GLU B 427 44.133 29.793 132.186 1.00 35.20 B O ATOM 2384 N GLY B 428 46.234 30.471 131.800 1.00 33.34 B N ATOM 2385 CA GLY B 428 46.041 31.692 132.561 1.00 34.51 B C ATOM 2386 C GLY B 428 46.066 31.428 134.057 1.00 36.70 B C ATOM 2387 O GLY B 428 46.241 30.281 134.475 1.00 35.95 B O ATOM 2388 N PRO B 429 45.887 32.468 134.893 1.00 37.61 B N ATOM 2389 CD PRO B 429 45.427 33.803 134.473 1.00 37.68 B C ATOM 2390 CA PRO B 429 45.888 32.363 136.361 1.00 35.27 B C ATOM 2391 CB PRO B 429 45.444 33.753 136.806 1.00 36.80 B C ATOM 2392 CG PRO B 429 44.594 34.224 135.655 1.00 38.82 B C ATOM 2393 C PRO B 429 44.969 3 1.258 136.882 1.00 34.51 B C ATOM 2394 O PRO B 429 43.769 31.248 136.605 1.00 35.20 B O ATOM 2395 N PRO B 430 45.533 30.312 137.648 1.00 32.84 B N ATOM 2396 CD PRO B 430 46.984 30.207 137.866 1.00 30.88 B C ATOM 2397 CA PRO B 430 44.843 29.160 138.246 1.00 33.23 B C ATOM 2398 CB PRO B 430 45.997 28.284 138.747 1.00 32.15 B C ATOM 2399 CG PRO B 430 47.172 28.722 137.930 1.00 32.06 B C ATOM 2400 C PRO B 430 43.870 29.482 139.381 1.00 33.86 B C ATOM 2401 O PRO B 430 42.786 28.891 139.475 1.00 32.09 B O ATOM 2402 N LEU B 431 44.271 30.405 140.250 1.00 34.56 B N ATOM 2403 CA LEU B 431 43.456 30.778 141.401 1.00 35.70 B C ATOM 2404 CB LEU B 431 44.300 31.550 142.419 1.00 33.79 B C ATOM 2405 CG LEU B 431 45.449 30.793 143.080 1.00 33.47 B C ATOM 2406 CD1 LEU B 431 46.049 31.651 144.190 1.00 33.46 B C ATOM 2407 CD2 LEU B 431 44.934 29.481 143.649 1.00 36.47 B C ATOM 2408 C LEU B 431 42.207 31.588 141.084 1.00 36.24 B C ATOM 2409 O LEU B 431 42.271 32.66 1140.479 1.00 36.37 B O ATOM 2410 N HIS B 432 41.064 31.064 141.505 1.00 36.71 B N ATOM 2411 CA HIS B 432 39.811 31.760 141.299 1.00 41.25 B C ATOM 2412 CB HIS B 432 38.662 30.761 141.191 1.00 40.99 B C ATOM 2413 GG HIS B 432 37.332 31.404 140.963 1.00 44.68 B C ATOM 2414 CD2 HIS B 432 36.589 31.541 139.838 1.00 44.42 B C ATOM 2415 ND1 HIS B 432 36.626 32.031 141.967 1.00 46.47 B N ATOM 2416 CE1 HIS B 432 35.504 32.524 141.472 1.00 45.59 B C ATOM 2417 NE2 HIS B 432 35.459 32.241 140.182 1.00 46.62 B N ATOM 2418 C HIS B 432 39.613 32.670 142.507 1.00 44.37 B C ATOM 2419 O HIS B 432 40.151 32.400 143.588 1.00 46.02 B O ATOM 2420 N LYS B 433 38.859 33.751 142.330 1.00 46.58 B N ATOM 2421 CA LYS B 433 38.627 34.678 143.428 1.00 46.70 B C ATOM 2422 CB LYS B 433 37.717 35.822 142.972 1.00 51.43 B C ATOM 2423 CG LYS B 433 38.355 36.668 141.865 1.00 55.90 B C ATOM 2424 CD LYS B 433 37.589 37.956 141.584 1.00 59.77 B C ATOM 2425 CE LYS B 433 38.320 38.811 140.549 1.00 61.80 B C ATOM 2426 NZ LYS B 433 37.720 40.171 140.380 1.00 62.64 B N ATOM 2427 C LYS B 433 38.062 33.973 144.658 1.00 43.89 B C ATOM 2428 O LYS B 433 38.150 34.491 145.767 1.00 44.99 B O ATOM 2429 N ASP B 434 37.501 32.783 144.460 1.00 40.87 B N ATOM 2430 CA ASP B 434 36.964 31.998 145.565 1.00 39.24 B C ATOM 2431 CB ASP B 434 36.032 30.905 145.038 1.00 38.77 B C ATOM 2432 CG ASP B 434 35.520 29.999 146.138 1.00 39.93 B C ATOM 2433 OD1 ASP B 434 36.053 28.882 146.286 1.00 43.55 B O ATOM 2434 OD2 ASP B 434 34.593 30.408 146.866 1.00 42.42 B O ATOM 2435 C ASP B 434 38.127 31.365 146.337 1.00 40.97 B C ATOM 2436 O ASP B 434 38.102 31.288 147.571 1.00 41.38 B O ATOM 2437 N ASP B 435 39.144 30.915 145.601 1.00 39.44 B N ATOM 2438 CA ASP B 435 40.324 30.305 146.204 1.00 37.18 B C ATOM 2439 CB ASP B 435 41.258 29.737 145.128 1.00 36.04 B C ATOM 2440 CG ASP B 435 40.608 28.653 144.293 1.00 37.10 B C ATOM 2441 OD1 ASP B 435 40.086 27.671 144.868 1.00 35.74 B O ATOM 2442 OD2 ASP B 435 40.632 28.779 143.050 1.00 40.79 B O ATOM 2443 C ASP B 435 41.088 31.354 147.007 1.00 38.01 B C ATOM 2444 O ASP B 435 41.591 31.077 148.098 1.00 39.15 B O ATOM 2445 N VAL B 436 41.178 32.560 146.459 1.00 37.34 B N ATOM 2446 CA VAL B 436 41.893 33.637 147.127 1.00 37.88 B C ATOM 2447 CB VAL B 436 42.018 34.863 146.209 1.00 37.00 B C ATOM 2448 CG1 VAL B 436 42.850 35.939 146.887 1.00 37.16 B C ATOM 2449 CG2 VAL B 436 42.654 34.454 144.893 1.00 37.45 B C ATOM 2450 C VAL B 436 41.203 34.051 148.426 1.00 41.35 B C ATOM 2451 O VAL B 436 41.870 34.444 149.392 1.00 40.58 B O ATOM 2452 N ASN B 437 39.872 33.964 148.445 1.00 42.61 B N ATOM 2453 CA ASN B 437 39.103 34.323 149.633 1.00 42.98 B C ATOM 2454 CB ASN B 437 37.602 34.372 149.331 1.00 44.38 B C ATOM 2455 CG ASN B 437 37.199 35.607 148.564 1.00 46.07 B C ATOM 2456 OD1 ASN B 437 37.778 36.681 148.743 1.00 49.54 B O ATOM 2457 ND2 ASN B 437 36.182 35.471 147.721 1.00 46.44 B N ATOM 2458 C ASN B 437 39.341 33.309 150.732 1.00 41.97 B C ATOM 2459 O ASN B 437 39.656 33.665 151.863 1.00 44.18 B O ATOM 2460 N GLY B 438 39.177 32.038 150.391 1.00 42.23 B N ATOM 2461 CA GLY B 438 39.373 30.980 151.364 1.00 41.20 B C ATOM 2462 C GLY B 438 40.737 31.015 152.030 1.00 40.27 B C ATOM 2463 O GLY B 438 40.851 30.821 153.241 1.00 40.43 B O ATOM 2464 N ILE B 439 41.778 31.269 151.246 1.00 39.21 B N ATOM 2465 CA ILE B 439 43.125 31.305 151.796 1.00 38.89 B C ATOM 2466 CB ILE B 439 44.195 31.186 150.666 1.00 34.85 B C ATOM 2467 CG2 ILE B 439 44.318 32.488 149.913 1.00 32.27 B C ATOM 2468 CG1 ILE B 439 45.546 30.783 151.262 1.00 34.00 B C ATOM 2469 CD1 ILE B 439 45.558 29.373 151.853 1.00 32.09 B C ATOM 2470 C ILE B 439 43.317 32.597 152.587 1.00 40.47 B C ATOM 2471 O ILE B 439 44.034 32.625 153.588 1.00 41.20 B O ATOM 2472 N ARG B 440 42.654 33.658 152.134 1.00 43.75 B N ATOM 2473 CA ARG B 440 42.725 34.967 152.782 1.00 44.46 B C ATOM 2474 CB ARG B 440 42.048 36.030 151.909 1.00 46.94 B C ATOM 2475 CG ARG B 440 42.937 37.185 151.471 1.00 49.56 B C ATOM 2476 CD ARG B 440 43.845 36.769 150.334 1.00 54.73 B C ATOM 2477 NE ARG B 440 44.726 37.850 149.901 1.00 58.03 B N ATOM 2478 CZ ARG B 440 44.306 38.991 149.362 1.00 60.42 B C ATOM 2479 NH1 ARG B 440 43.009 39.211 149.186 1.00 60.93 B N ATOM 2480 NH2 ARG B 440 45.188 39.910 148.988 1.00 60.50 B N ATOM 2481 C ARG B 440 42.006 34.908 154.128 1.00 44.17 B C ATOM 2482 O ARG B 440 42.320 35.666 155.047 1.00 43.24 B O ATOM 2483 N HIS B 441 41.033 34.004 154.221 1.00 42.88 B N ATOM 2484 CA HIS B 441 40.235 33.818 155.428 1.00 43.46 B C ATOM 2485 CB HIS B 441 38.997 32.972 155.112 1.00 46.73 B C ATOM 2486 CG HIS B 441 38.118 32.713 156.297 1.00 52.22 B C ATOM 2487 CD2 HIS B 441 37.906 31.588 157.022 1.00 53.91 B C ATOM 2488 ND1 HIS B 441 37.331 33.690 156.871 1.00 54.78 B N ATOM 2489 CE1 HIS B 441 36.673 33.178 157.896 1.00 54.20 B C ATOM 2490 NB2 HIS B 441 37.005 31.904 158.010 1.00 54.76 B N ATOM 2491 C HIS B 441 41.029 33.144 156.538 1.00 42.38 B C ATOM 2492 O HIS B 441 40.835 33.448 157.713 1.00 43.43 B O ATOM 2493 N LEU B 442 41.924 32.233 156.158 1.00 40.54 B N ATOM 2494 CA LEU B 442 42.747 31.495 157.118 1.00 37.84 B C ATOM 2495 CB LEU B 442 43.136 30.124 156.542 1.00 36.23 B C ATOM 2496 CG LEU B 442 42.020 29.121 156.224 1.00 36.95 B C ATOM 2497 CD1 LEU B 442 42.600 27.921 155.494 1.00 37.45 B C ATOM 2498 CD2 LEU B 442 41.337 28.676 157.507 1.00 38.67 B C ATOM 2499 C LEU B 442 44.012 32.232 157.548 1.00 35.29 B C ATOM 2500 O LEU B 442 44.367 32.218 158.721 1.00 37.44 B O ATOM 2501 N TYR B 443 44.693 32.872 156.605 1.00 34.38 B N ATOM 2502 CA TYR B 443 45.932 33.581 156.920 1.00 36.23 B C ATOM 2503 CB TYR B 443 47.105 32.984 156.123 1.00 34.25 B C ATOM 2504 CG TYR B 443 47.261 31.490 156.300 1.00 31.93 B C ATOM 2505 CD1 TYR B 443 46.614 30.596 155.446 1.00 29.81 B C ATOM 2506 CE1 TYR B 443 46.695 29.215 155.649 1.00 28.03 B C ATOM 2507 CD2 TYR B 443 48.004 30.968 157.366 1.00 29.17 B C ATOM 2508 CE2 TYR B 443 48.092 29.592 157.578 1.00 28.10 B C ATOM 2509 CZ TYR B 443 47.433 28.721 156.718 1.00 29.15 B C ATOM 2510 OH TYR B 443 47.496 27.360 156.932 1.00 27.85 B O ATOM 2511 C TYR B 443 45.855 35.082 156.659 1.00 38.24 B C ATOM 2512 O TYR B 443 46.801 35.794 157.063 1.00 40.58 B O ATOM 2513 OT TYR B 443 44.864 35.527 156.044 1.00 41.15 B O ATOM 2562 ZN ZN B 1 41.275 17.840 146.537 1.00 30.01 Z ZN ATOM 2563 ZN ZN B 2 49.676 8.887 150.296 1.00 22.73 Z ZN ATOM 2570 CA CA B 3 54.013 17.086 157.486 1.00 25.83 C C ATOM 2571 CA CA B 4 54.046 8.303 135.827 1.00 47.76 C C ATOM 2572 CA CA B 5 50.701 18.541 128.694 1.00 57.49 C C ATOM 2569 CA CA B 6 45.250 7.241 139.948 1.00 21.01 C C ATOM 2574 CA CA B 7 53.492 38.165 150.097 1.00 99.62 C C ATOM 2537 C1 FRA B 2 40.988 17.843 141.282 1.00 21.42 M C ATOM 2538 C2 FRA B 2 42.202 16.892 141.164 1.00 23.04 M C ATOM 2539 C3 FRA B 2 43.397 17.813 140.945 1.00 21.68 M C ATOM 2540 C4 FRA B 2 42.395 16.088 142.486 1.00 20.53 M C ATOM 2541 C5 FRA B 2 41.287 15.047 142.944 1.00 22.68 M C ATOM 2542 C6 FRA B 2 −41.674 14.384 144.328 1.00 21.04 M C ATOM 2543 N7 FRA B 2 41.894 15.346 145.441 1.00 26.66 M N ATOM 2544 O8 FRA B 2 40.878 16.003 145.917 1.00 16.04 M O ATOM 2545 C9 FRA B 2 43.101 15.578 145.982 1.00 25.43 M C ATOM 2546 O10 FRA B 2 43.304 16.343 146.865 1.00 27.78 M O ATOM 2547 C11 FRA B 2 41.103 13.852 141.935 1.00 24.21 M C ATOM 2548 N12 FRA B 2 39.910 13.731 141.312 1.00 24.87 M N ATOM 2549 C13 FRA B 2 39.558 12.636 140.307 1.00 25.69 M C ATOM 2550 C14 FRA B 2 38.064 12.068 140.550 1.00 26.41 M C ATOM 2551 C15 FRA B 2 37.671 10.934 139.534 1.00 23.54 M C ATOM 2552 C16 FRA B 2 36.936 13.161 140.404 1.00 25.14 M C ATOM 2553 C17 FRA B 2 37.918 11.501 141.991 1.00 25.52 M C ATOM 2554 C18 FRA B 2 39.789 13.241 138.843 1.00 26.03 M C ATOM 2555 O19 FRA B 2 39.414 14.401 138.550 1.00 27.42 M O ATOM 2556 N20 FRA B 2 40.416 12.393 137.981 1.00 25.15 M N ATOM 2557 C21 FRA B 2 40.752 12.702 136.573 1.00 30.05 M C ATOM 2558 O22 FRA B 2 42.049 13.051 141.732 1.00 25.04 M O ATOM 2576 O HOH W 1 53.372 24.644 125.318 1.00 1.00 W O ATOM 2577 O HOH W 2 74.083 20.414 120.913 1.00 21.76 W O ATOM 2578 O HOH W 3 49.364 12.911 104.335 1.00 26.01 W O ATOM 2579 O HOH W 4 52.144 16.494 124.475 1.00 14.30 W O ATOM 2580 O HOH W 5 58.587 7.0141 15.292 1.00 27.11 W O ATOM 2581 O HOH W 6 75.605 18.864 112.249 1.00 18.56 W O ATOM 2582 O HOH W 7 65.295 7.257 120.405 1.00 1.00 W O ATOM 2583 O HOH W 8 57.185 8.107 113.191 1.00 17.03 W O ATOM 2584 O HON W 9 64.469 12.077 98.818 1.00 47.82 W O ATOM 2585 O HOH W 10 51.666 21.908 124.829 1.00 15.33 W O ATOM 2586 O HOH W 11 67.629 24.639 127.665 1.00 20.55 W O ATOM 2587 O HOH W 12 67.365 14.751 108.625 1.00 21.02 W O ATOM 2588 O HOH W 13 52.957 12.041 116.137 1.00 15.20 W O ATOM 2589 O HOH W 14 51.253 9.646 116.663 1.00 29.59 W O ATOM 2590 O HOH W 15 48.380 16.148 113.137 1.00 26.43 W O ATOM 2591 O HOH W 16 49.177 9.855 111.408 1.00 25.21 W O ATOM 2592 O HOH W 17 56.870 18.582 90.415 1.00 50.62 W O ATOM 2593 O HOH W 18 56.995 17.921 96.140 1.00 26.85 W O ATOM 2594 O HOH W 19 61.756 9.877 125.515 1.00 40.50 W O ATOM 2595 O HOH W 20 45.873 28.448 97.477 1.00 25.98 W O ATOM 2596 O HOH W 21 50.275 10.441 122.477 1.00 33.64 W O ATOM 2597 O HOH W 22 56.828 39.659 107.746 1.00 37.53 W O ATOM 2598 O HOH W 23 56.922 8.730 101.984 1.00 51.25 W O ATOM 2599 O HOH W 24 63.090 12.420 103.873 1.00 23.17 W O ATOM 2600 O HOH W 25 78.432 18.341 111.530 1.00 33.10 W O ATOM 2601 O HOH W 26 55.278 7.063 126.543 1.00 22.51 W O ATOM 2602 O HOH W 27 71.699 14.944 110.281 1.00 31.13 W O ATOM 2603 O HOH W 28 65.856 12.461 105.207 1.00 34.23 W O ATOM 2604 O HOH W 29 49.226 13.404 112.556 1.00 36.10 W O ATOM 2605 O HOH W 30 45.806 26.797 113.582 1.00 25.06 W O ATOM 2606 O HOH W 31 50.921 22.489 96.419 1.00 38.17 W O ATOM 2607 O HOH W 32 47.043 17.179 110.619 1.00 27.88 W O ATOM 2608 O HOH W 33 50.505 31.197 136.475 1.00 33.10 W O ATOM 2609 O HOH W 34 47.341 22.271 121.211 1.00 20.31 W O ATOM 2610 O HOH W 35 61.912 15.434 101.221 1.00 22.75 W O ATOM 2611 O HOH W 36 70.118 14.389 108.156 1.00 55.54 W O ATOM 2612 O HOH W 37 60.170 4.215 113.980 1.00 40.21 W O ATOM 2613 O HOH W 38 50.540 23.541 133.215 1.00 2.46 W O ATOM 2614 O HOH W 39 48.871 4.037 141.580 1.00 13.61 W O ATOM 2615 O HOH W 40 59.625 29.594 154.497 1.00 17.76 W O ATOM 2616 O HOH W 41 58.300 23.513 135.522 1.00 22.04 W O ATOM 2617 O HOH W 42 64.850 17.232 147.313 1.00 21.84 W O ATOM 2618 O HOH W 43 49.326 3.982 150.548 1.00 24.48 W O ATOM 2619 O HOH W 45 63.774 19.112 148.870 1.00 12.98 W O ATOM 2620 O HOH W 46 55.863 15.629 163.760 1.00 28.09 W O ATOM 2621 O HOH W 47 53.389 24.883 133.848 1.00 20.87 W O ATOM 2622 O HOH W 48 47.215 9.463 133.451 1.00 38.63 W O ATOM 2623 O HOH W 49 54.340 11.753 153.786 1.00 25.99 W O ATOM 2624 O HOH W 50 61.472 23.563 144.309 1.00 18.90 W O ATOM 2625 O HOH W 51 63.912 24.339 144.017 1.00 19.40 W O ATOM 2626 O HOH W 52 58.245 29.246 145.388 1.00 26.64 W O ATOM 2627 O HOH W 53 63.745 27.746 148.959 1.00 20.88 W O ATOM 2628 O HOH W 54 51.102 26.318 167.875 1.00 28.44 W O ATOM 2629 O HOH W 55 52.106 25.451 162.757 1.00 26.05 W O ATOM 2630 O HOH W 56 62.401 12.111 136.745 1.00 22.15 W O ATOM 2631 O HOH W 57 45.079 38.240 157.288 1.00 46.25 W O ATOM 2632 O HOH W 58 64.533 23.652 138.613 1.00 23.45 W O ATOM 2633 O HOH W 59 32.586 28.259 147.755 1.00 53.44 W O ATOM 2634 O HOH W 60 60.965 22.491 159.169 1.00 36.88 W O ATOM 2635 O HOH W 61 56.540 16.675 157.926 1.00 22.67 W O ATOM 2636 O HOH W 62 49.724 1.457 152.163 1.00 31.25 W O ATOM 2637 O HOH W 63 66.979 17.779 135.834 1.00 30.64 W O ATOM 2638 O HOH W 64 53.679 7.411 152.678 1.00 24.59 W O ATOM 2639 O HOH W 65 55.862 13.242 157.045 1.00 22.19 W O ATOM 2640 O HOH W 66 60.317 27.514 146.861 1.00 50.28 W O ATOM 2641 O HOH W 67 48.564 34.049 142.813 1.00 37.03 W O ATOM 2642 O HOH W 68 47.734 34.009 159.841 1.00 57.14 W O ATOM 2643 O HOH W 69 56.949 31.429 147.112 1.00 30.39 W O ATOM 2644 O HOH W 70 47.008 25.477 120.702 1.00 23.76 W O ATOM 2645 O HOH W 71 53.453 29.741 136.903 1.00 25.90 W O ATOM 2646 O HOH W 72 54.023 18.711 159.706 1.00 18.27 W O ATOM 2647 O HOH W 73 54.530 9.056 154.663 1.00 34.56 W O ATOM 2648 O HOH W 74 66.399 14.925 149.889 1.00 36.21 W O ATOM 2649 O HOH W 75 56.078 0.717 148.547 1.00 47.62 W O ATOM 2650 O HOH W 76 55.037 3.104 145.929 1.00 22.70 W O ATOM 2651 O HOH W 77 57.979 5.727 117.915 1.00 65.95 W O ATOM 2652 O HOH W 78 38.602 9.525 136.215 1.00 34.41 W O ATOM 2653 O HOH W 79 56.644 33.927 107.571 1.00 25.40 W O ATOM 2654 O HOH W 80 56.901 12.608 98.500 1.00 45.22 W O ATOM 2655 O HOH W 81 66.159 25.939 129.659 1.00 45.73 W O ATOM 2656 O HOH W 82 52.849 33.406 118.492 1.00 33.45 W O ATOM 2657 O HOH W 83 40.064 12.132 132.917 1.00 45.44 W O ATOM 2658 O HOH W 84 61.356 7.072 144.041 1.00 52.29 W O ATOM 2659 O HOH W 85 59.332 33.793 126.661 1.00 37.65 W O ATOM 2660 O HOH W 86 76.248 14.005 117.780 1.00 38.05 W O ATOM 2661 O HOH W 87 63.920 4.959 114.145 1.00 28.43 W O ATOM 2662 O HOH W 88 41.594 23.567 106.694 1.00 35.95 W O ATOM 2663 O HOH W 89 43.961 20.340 105.825 1.00 34.92 W O ATOM 2664 O HOH W 90 73.852 13.594 117.386 1.00 26.01 W O ATOM 2665 O HOH W 91 59.941 14.152 100.157 1.00 27.50 W O ATOM 2666 O HOH W 92 59.242 23.420 132.602 1.00 16.67 W O ATOM 2667 O HOH W 93 58.837 25.317 128.952 1.00 21.05 W O ATOM 2668 O HOH W 94 51.613 25.829 131.530 1.00 40.97 W O ATOM 2669 O HOH W 95 64.674 28.352 131.418 1.00 31.06 W O ATOM 2670 O HOH W 96 60.935 29.269 136.385 1.00 24.27 W O ATOM 2671 O HOH W 97 54.832 34.703 109.520 1.00 17.56 W O ATOM 2672 O HOH W 98 58.791 32.739 117.544 1.00 24.04 W O ATOM 2673 O HOH W 99 56.442 35.249 118.352 1.00 28.89 W O ATOM 2674 O HOH W 100 46.526 37.510 114.770 1.00 35.71 W O ATOM 2675 O HOH W 101 54.579 35.72 1151.192 1.00 51.01 W O ATOM 2676 O HOH W 102 58.105 32.269 149.264 1.00 23.65 W O ATOM 2677 O HOH W 103 65.313 13.049 157.092 1.00 26.96 W O ATOM 2678 O HOH W 104 66.201 11.386 155.250 1.00 48.24 W O ATOM 2679 O HOH W 105 53.996 0.840 145.922 1.00 34.76 W O ATOM 2680 O HOH W 106 46.202 0.833 136.125 1.00 47.74 W O ATOM 2681 O HOH W 107 56.086 6.461 135.385 1.00 47.82 W O ATOM 2682 O HOH W 108 51.570 16.588 127.129 1.00 18.01 W O ATOM 2683 O HOH W 109 46.668 19.140 128.889 1.00 23.88 W O ATOM 2684 O HOH W 110 45.451 12.416 128.248 1.00 32.22 W O ATOM 2685 O HOH W 111 53.514 30.754 139.864 1.00 31.81 W O ATOM 2686 O HOH W 112 52.273 39.562 147.763 1.00 51.12 W O ATOM 2687 O HOH W 113 52.591 10.981 161.536 1.00 34.69 W O ATOM 2688 O HOH W 114 50.264 24.639 126.956 1.00 19.43 W O ATOM 2689 O HOH W 115 45.122 15.259 128.545 1.00 36.82 W O ATOM 2690 O HOH W 116 45.881 15.698 122.389 1.00 39.53 W O ATOM 2691 O HOH W 117 45.448 17.802 130.938 1.00 37.87 W O ATOM 2692 O HOH W 118 58.454 6.855 127.071 1.00 27.25 W O ATOM 2693 O HOH W 119 62.131 28.235 104.517 1.00 40.71 W O ATOM 2694 O HOH W 120 66.292 32.682 114.288 1.00 25.89 W O ATOM 2695 O HOH W 121 65.759 26.751 110.354 1.00 19.28 W O END

[0135] TABLE 3 Three dimensional atomic coordinates of the MMP9 mutant (E402Q construct in complex with the reverse hydroxamate compound of Formula I. REMARK coordinates from restrained individual B-factor refinement. REMARK refinement resolution: 100 -2.3 A REMARK starting r = 0.2096 free_r = 0.2397 REMARK final r = 0.2074 free_r = 0.2408 REMARK B rmsd for bonded mainchain atoms = 1.707 target = 1.5 REMARK B rmsd for bonded sidechain atoms = 2.673 target = 2.0 REMARK B rmsd for angle mainchain atoms = 2.714 target = 2.0 REMARK B rmsd for angle sidechain atoms = 3.856 target = 2.5 REMARK wa = 2.19316 REMARK rweight = 5.978512E−02 REMARK target = mlf steps = 30 REMARK sg = P4(1)2(1)2 a = 56.005 b = 56.005 c = 262.655 alpha = 90 beta = 90 gamma = 9 REMARK parameter file 1: MSI_CNX_TOPPAR: protein_rep.param REMARK parameter file 2: MSI_CNX_TOPPAR: ion.param REMARK parameter file 3: MSI_CNX_TOPPAR: water_rep.param REMARK parameter file 4: fra.par REMARK molecular structure file: mmp9.mtf REMARK input coordinates: anneal_restrain_1.pdb REMARK reflection file = mmp9_rf.hkl REMARK ncs = restrain ncs file = ncs_restrain.def REMARK B-correction resolution: 6.0-2.3 REMARK initial B-factor correction applied to fobs: REMARK B11 = −4.644 B22 = −4.644 B33 = 9.288 REMARK B12 = 0.000 B13 = 0.000 B23 = 0.000 REMARK B-factor correction applied to coordinate array B: 0.533 REMARK bulk solvent: (Mask) density level 0.372729 e/A{circumflex over ( )}3, B-factor 48.8354 A{circumflex over ( 2)} REMARK reflections with |Fobs|/sigma_F < 0.0 rejected REMARK reflections with |Fobs| > 1000 * rms(Fobs) rejected REMARK theoretical total number of refl. in resol. range: 19670 (100.0%) REMARK number of unobserved reflections (no entry or |F| =0): 2295 (11.7%) REMARK number of reflections rejected: 0(0.0%) REMARK total number of reflections used: 17375 (88.3%) REMARK number of reflections in working set: 16691 (84.9%) REMARK number of reflections in test set: 684 (3.5%) REMARK FILENAME = ″bindividual7.pdb″ REMARK DATE: Nov. 30, 2000 13:59:53 created by user: sian REMARK Written by CNX VBRSION: 2000 CRYST1 56.005 56.005 262.655 90.00 90.00 90.00 P 41 21 2 SCALE1 0.017856 0.000000 0.000000  0.00000 SCALE2 0.000000 0.017856 0.000000  0.00000 SCALE3 0.000000 0.000000 0.003807  0.00000 ATOM 1 CB PHE A 110 68.144 27.293 107.042 1.00 76.67 A C ATOM 2 CG FHE A 110 69.059 26.231 107.577 1.00 76.83 A C ATOM 3 CD1 PHE A 110 70.433 26.309 107.372 1.00 76.63 A C ATOM 4 CD2 PHE A 110 68.547 25.145 108.276 1.00 76.62 A C ATOM S CE1 PHE A 110 71.282 25.322 107.853 1.00 75.40 A C ATOM 6 CE2 PHE A 110 69.390 24.152 108.763 1.00 76.11 A C ATOM 7 CZ PHE A 110 70.760 24.241 108.550 1.00 75.74 A C ATOM 8 C PHE A 110 67.022 28.261 105.029 1.00 76.18 A C ATOM 9 O PHE A 110 65.965 28.280 105.664 1.00 76.86 A O ATOM 10 N PHE A 110 69.510 28.084 105.133 1.00 76.75 A N ATOM 11 CA PHE A 110 68.217 27.455 105.522 1.00 76.45 A C ATOM 12 N GLU A 111 67.204 28.928 103.893 1.00 74.63 A N ATOM 13 CA GLU A 111 66.148 29.724 103.279 1.00 73.01 A C ATOM 14 CB GLU A 111 66.490 31.215 103.335 1.00 75.82 A C ATOM 15 CO GLU A 111 66.819 31.745 104.726 1.00 80.41 A C ATOM 16 CD GLU A 111 65.689 31.554 105.725 1.00 83.58 A C ATOM 17 OE1 GLU A 111 64.561 32.022 105.452 1.00 85.28 A O ATOM 18 OE2 GLU A 111 65.934 30.941 106.789 1.00 84.02 A O ATOM 19 C GLU A 111 66.025 29.282 101.826 1.00 69.95 A C ATOM 20 O GLU A 111 67.025 29.180 101.111 1.00 70.43 A O ATOM 21 N GLY A 112 64.801 29.009 101.394 1.00 66.03 A N ATOM 22 CA GLY A 112 64.587 28.577 100.027 1.00 60.34 A C ATOM 23 C GLY A 112 63.299 29.143 99.479 1.00 56.89 A C ATOM 24 O GLY A 112 62.515 29.744 100.213 1.00 57.97 A O ATOM 25 N ASP A 113 63.077 28.955 98.185 1.00 53.94 A N ATOM 26 CA ASP A 113 61.866 29.459 97.553 1.00 50.40 A C ATOM 27 CB ASP A 113 62.209 30.556 96.543 1.00 52.58 A C ATOM 28 CG ASP A 113 62.790 31.792 97.202 1.00 53.44 A C ATOM 29 OD1 ASP A 113 62.092 32.405 98.039 1.00 53.76 A O ATOM 30 OD2 ASP A 113 63.944 32.146 96.885 1.00 53.72 A O ATOM 31 C ASP A 113 61.098 28.345 96.867 1.00 46.20 A C ATOM 32 O ASP A 113 60.589 28.519 95.763 1.00 46.06 A O ATOM 33 N LEU A 114 61.024 27.198 97.535 1.00 40.51 A N ATOM 34 CA LEU A 114 60.309 26.043 97.018 1.00 35.29 A C ATOM 35 CB LEU A 114 61.265 24.870 96.812 1.00 35.18 A C ATOM 36 CG LEU A 114 62.424 25.022 95.829 1.00 35.74 A C ATOM 37 CD1 LEU A 114 63.155 23.689 95.726 1.00 34.64 A C ATOM 38 CD2 LEU A 114 61.906 25.455 94.463 1.00 31.83 A C ATOM 39 C LEU A 114 59.229 25.624 98.003 1.00 33.60 A C ATOM 40 O LEU A 114 59.363 25.842 99.205 1.00 33.68 A O ATOM 41 N LYS A 115 58.151 25.040 97.489 1.00 30.09 A N ATOM 42 CA LYS A 115 57.066 24.556 98.331 1.00 28.79 A C ATOM 43 CB LYS A 115 55.782 25.350 98.091 1.00 27.23 A C ATOM 44 CG LYS A 115 55.136 25.113 96.739 1.00 30.27 A C ATOM 45 CD LYS A 115 53.726 25.671 96.711 1.00 31.99 A C ATOM 46 CE LYS A 115 53.015 25.309 95.420 1.00 33.32 A C ATOM 47 NZ LYS A 115 51.602 25.772 95.434 1.00 31.74 A N ATOM 48 C LYS A 115 56.854 23.099 97.946 1.00 27.74 A C ATOM 49 O LYS A 115 57.490 22.610 97.017 1.00 26.52 A O ATOM 50 N TRP A 116 55.984 22.398 98.660 1.00 26.86 A N ATOM 51 CA TRP A 116 55.725 21.005 98.327 1.00 26.50 A C ATOM 52 CB TRP A 116 55.139 20.242 99.525 1.00 24.26 A C ATOM 53 CG TRP A 116 56.071 20.142 100.708 1.00 26.96 A C ATOM 54 CD2 TRP A 116 57.243 19.321 100.810 1.00 26.47 A C ATOM 55 CE2 TRP A 116 57.806 19.554 102.087 1.00 25.23 A C ATOM 56 CE3 TRP A 116 57.873 18.414 99.946 1.00 25.47 A C ATOM 57 CD1 TRP A 116 55.977 20.821 101.894 1.00 23.47 A C ATOM 58 NE1 TRP A 116 57.014 20.472 102.724 1.00 22.33 A N ATOM 59 CZ2 TRP A 116 58.972 18.910 102.521 1.00 24.08 A C ATOM 60 CZ3 TRP A 116 59.037 17.774 100.378 1.00 24.64 A C ATOM 61 CH2 TRP A 116 59.572 18.027 101.654 1.00 25.34 A C ATOM 62 C TRP A 116 54.723 20.991 97.184 1.00 27.50 A C ATOM 63 O TRP A 116 53.828 21.836 97.125 1.00 25.79 A O ATOM 64 N HIS A 117 54.877 20.039 96.271 1.00 27.87 A N ATOM 65 CA HIS A 117 53.950 19.932 95.158 1.00 29.48 A C ATOM 66 CB HIS A 117 54.692 19.528 93.885 1.00 25.71 A C ATOM 67 CG HIS A 117 55.384 20.674 93.214 1.00 27.00 A C ATOM 68 CD2 HIS A 117 55.394 21.998 93.501 1.00 27.93 A C ATOM 69 ND1 HIS A 117 56.184 20.520 92.103 1.00 28.15 A N ATOM 70 CE1 HIS A 117 56.659 21.697 91.736 1.00 25.56 A C ATOM 71 NE2 HIS A 117 56.195 22.611 92.568 1.00 25.76 A N ATOM 72 C HIS A 117 52.794 18.982 95.465 1.00 31.31 A C ATOM 73 O HIS A 117 51.849 18.873 94.687 1.00 36.62 A O ATOM 74 N HIS A 118 52.868 18.292 96.600 1.00 28.91 A N ATOM 75 CA HIS A 118 51.782 17.412 97.007 1.00 27.75 A C ATOM 76 CB HIS A 118 52.257 15.966 97.160 1.00 26.46 A C ATOM 77 CG HIS A 118 53.454 15.800 98.041 1.00 28.06 A C ATOM 78 CD2 HIS A 118 53.587 15.230 99.262 1.00 26.27 A C ATOM 79 ND1 HIS A 118 54.715 16.213 97.672 1.00 27.31 A N ATOM 80 CE1 HIS A 118 55.575 15.901 98.625 1.00 25.21 A C ATOM 81 NE2 HIS A 118 54.916 15.304 99.600 1.00 25.44 A N ATOM 82 C HIS A 118 51.232 17.949 98.322 1.00 28.02 A C ATOM 83 O HIS A 118 51.906 18.717 99.006 1.00 30.48 A O ATOM 84 N HIS A 119 50.008 17.566 98.670 1.00 28.21 A N ATOM 85 CA HIS A 119 49.394 18.049 99.900 1.00 28.31 A C ATOM 86 CB HIS A 119 48.001 18.597 99.607 1.00 27.88 A C ATOM 87 CG HIS A 119 48.015 19.881 98.843 1.00 30.03 A C ATOM 88 CD2 HIS A 119 49.045 20.642 98.402 1.00 28.56 A C ATOM 89 ND1 HIS A 119 46.862 20.530 98.452 1.00 32.34 A N ATOM 90 CE1 HIS A 119 47.182 21.636 97.804 1.00 30.91 A C ATOM 91 NE2 HIS A 119 48.500 21.728 97.760 1.00 30.11 A N ATOM 92 C HIS A 119 49.318 17.040 101.034 1.00 28.11 A C ATOM 93 O HIS A 119 49.120 17.424 102.184 1.00 28.79 A O ATOM 94 N ASN A 120 49.447 15.757 100.715 1.00 28.28 A N ATOM 95 CA ASN A 120 49.418 14.724 101.742 1.00 30.67 A C ATOM 96 CB ASN A 120 48.753 13.442 101.206 1.00 35.59 A C ATOM 97 CG ASN A 120 49.339 12.970 99.874 1.00 40.97 A C ATOM 98 OD1 ASN A 120 49.628 13.776 98.982 1.00 42.91 A O ATOM 99 ND2 ASN A 120 49.494 11.652 99.728 1.00 42.68 A N ATOM 100 C ASN A 120 50.873 14.489 102.141 1.00 29.30 A C ATOM 101 O ASN A 120 51.564 13.634 101.585 1.00 29.67 A O ATOM 102 N ILE A 121 51.330 15.287 103.103 1.00 26.98 A N ATOM 103 CA ILE A 121 52.710 15.233 103.577 1.00 26.04 A C ATOM 104 CB ILE A 121 53.138 16.617 104.109 1.00 26.73 A C ATOM 105 CG2 ILE A 121 54.574 16.568 104.626 1.00 26.58 A C ATOM 106 CG1 ILE A 121 52.997 17.650 102.987 1.00 29.00 A C ATOM 107 CD1 ILE A 121 53.451 19.037 103.357 1.00 32.81 A C ATOM 108 C ILE A 121 52.945 14.179 104.650 1.00 23.95 A C ATOM 109 O ILE A 121 52.081 13.928 105.484 1.00 24.37 A O ATOM 110 N THR A 122 54.119 13.560 104.621 1.00 20.08 A N ATOM 111 CA THR A 122 54.441 12.534 105.598 1.00 21.17 A C ATOM 112 CB THR A 122 54.763 11.172 104.914 1.00 22.42 A C ATOM 113 OG1 THR A 122 55.948 11.294 104.115 1.00 20.53 A O ATOM 114 CG2 THR A 122 53.592 19.722 104.042 1.00 21.00 A C ATOM 115 C THR A 122 55.624 12.925 106.481 1.00 20.68 A C ATOM 116 O THR A 122 56.502 13.706 106.081 1.00 18.28 A O ATOM 117 N TYR A 123 55.640 12.382 107.693 1.00 18.69 A N ATOM 118 CA TYR A 123 56.728 12.671 108.612 1.00 17.02 A C ATOM 119 CB TYR A 123 56.374 13.828 109.561 1.00 12.64 A C ATOM 120 CG TYR A 123 55.291 13.533 110.579 1.00 14.99 A C ATOM 121 CD1 TYR A 123 53.949 13.737 110.277 1.00 15.83 A C ATOM 122 CE1 TYR A 123 52.953 13.517 111.228 1.00 14.44 A C ATOM 123 CD2 TYR A 123 55.613 13.088 111.867 1.00 15.15 A C ATOM 124 CE2 TYR A 123 54.623 12.866 112.821 1.00 13.15 A C ATOM 125 CZ TYR A 123 53.296 13.087 112.495 1.00 14.54 A C ATOM 126 OH TYR A 123 52.305 12.912 113.439 1.00 17.15 A O ATOM 127 C TYR A 123 57.109 11.446 109.419 1.00 15.63 A C ATOM 128 O TYR A 123 56.277 10.594 109.735 1.00 14.88 A O ATOM 129 N TRP A 124 58.387 11.380 109.745 1.00 14.30 A N ATOM 130 CA TRP A 124 58.933 10.288 110.504 1.00 15.16 A C ATOM 131 CB TRP A 124 59.876 9.486 109.603 1.00 17.22 A C ATOM 132 CG TRP A 124 60.649 8.390 110.274 1.00 14.19 A C ATOM 133 CD2 TRP A 124 62.005 8.019 110.004 1.00 17.22 A C ATOM 134 CE2 TRP A 124 62.299 6.892 110.807 1.00 18.18 A C ATOM 135 CE3 TRP A 124 63.002 8.525 109.157 1.00 17.93 A C ATOM 136 CD1 TRP A 124 60.186 7.506 111.204 1.00 15.79 A C ATOM 137 NE1 TRP A 124 61.172 6.599 111.530 1.00 17.60 A N ATOM 138 CZ2 TRP A 124 63.548 6.262 110.788 1.00 17.69 A C ATOM 139 CZ3 TRP A 124 64.244 7.899 109.139 1.00 22.22 A C ATOM 140 CH2 TRP A 124 64.505 6.776 109.951 1.00 19.94 A C ATOM 141 C TRP A 124 59.679 10.821 111.720 1.00 15.01 A C ATOM 142 O TRP A 124 60.575 11.645 111.590 1.00 15.43 A O ATOM 143 N ILE A 125 59.283 10.365 112.903 1.00 13.81 A N ATOM 144 CA ILB A 125 59.960 10.754 114.127 1.00 14.20 A C ATOM 145 CB ILE A 125 59.009 10.697 115.341 1.00 14.44 A C ATOM 146 CG2 ILE A 125 59.758 11.087 116.609 1.00 10.86 A C ATOM 147 CG1 ILB A 125 57.833 11.649 115.110 1.00 14.53 A C ATOM 148 CD1 ILE A 125 56.721 11.500 116.106 1.00 16.01 A C ATOM 149 C ILE A 125 61.038 9.685 114.249 1.00 14.73 A C ATOM 150 O ILE A 125 60.763 8.564 114.660 1.00 17.21 A O ATOM 151 N GLN A 126 62.259 10.036 113.863 1.00 15.17 A N ATOM 152 CA GLN A 126 63.374 9.102 113.877 1.00 17.19 A C ATOM 153 CB GLN A 126 64.540 9.679 113.065 1.00 15.71 A C ATOM 154 CG GLN A 126 65.810 8.849 113.134 1.00 19.08 A C ATOM 155 CD GLN A 126 67.006 9.537 112.492 1.00 21.76 A C ATOM 156 OB1 GLN A 126 68.141 9.434 112.978 1.00 21.48 A O ATOM 157 NE2 GLN A 126 66.762 10.235 111.395 1.00 21.97 A N ATOM 158 C GLN A 126 63.858 8.702 115.270 1.00 18.20 A C ATOM 159 O GLN A 126 64.062 7.519 115.536 1.00 18.29 A O ATOM 160 N ASN A 127 64.066 9.681 116.145 1.00 19.88 A N ATOM 161 CA ASN A 127 64.515 9.397 117.504 1.00 18.22 A C ATOM 162 CB ASN A 127 66.942 9.423 117.594 1.00 19.01 A C ATOM 163 CG ASN A 127 66.631 10.770 117.242 1.00 21.39 A C ATOM 164 OD1 ASN A 127 65.957 11.798 117.310 1.00 25.90 A O ATOM 165 ND2 ASN A 127 67.909 10.774 116.880 1.00 20.17 A N ATOM 166 C ASN A 127 63.900 10.386 118.483 1.00 19.18 A C ATOM 167 O ASN A 127 63.238 11.341 118.068 1.00 18.72 A O ATOM 168 N TYR A 128 64.128 10.163 119.779 1.00 17.90 A N ATOM 169 CA TYR A 128 63.539 11.006 120.822 1.00 15.61 A C ATOM 170 CB TYR A 128 62.592 10.166 121.693 1.00 15.35 A C ATOM 171 CG TYR A 128 61.389 9.623 120.957 1.00 14.14 A C ATOM 172 CD1 TYR A 128 61.476 8.467 120.178 1.00 12.53 A C ATOM 173 CE1 TYR A 128 60.374 8.000 119.469 1.00 12.28 A C ATOM 174 CD2 TYR A 128 60.172 10.293 121.008 1.00 12.14 A C ATOM 175 CE2 TYR A 128 59.078 9.839 120.306 1.00 14.27 A C ATOM 176 CZ TYR A 128 59.182 8.698 119.539 1.00 13.46 A C ATOM 177 OH TYR A 128 58.084 8.292 118.837 1.00 12.04 A O ATOM 178 C TYR A 128 64.501 11.716 121.746 1.00 14.76 A C ATOM 179 O TYR A 128 65.681 11.396 121.808 1.00 15.87 A O ATOM 180 N SER A 129 63.969 12.693 122.471 1.00 17.19 A N ATOM 181 CA SER A 129 64.742 13.430 123.460 1.00 19.66 A C ATOM 182 CB SER A 129 64.173 14.826 123.675 1.00 17.51 A C ATOM 183 OG SER A 129 64.731 15.394 124.844 1.00 16.48 A O ATOM 184 C SER A 129 64.600 12.640 124.753 1.00 22.10 A C ATOM 185 O SER A 129 63.646 11.882 124.920 1.00 21.65 A O ATOM 186 N GLU A 130 65.529 12.821 125.677 1.00 24.54 A N ATOM 187 CA GLU A 130 65.459 12.085 126.925 1.00 28.04 A C ATOM 188 CB GLU A 130 66.884 11.859 127.459 1.00 31.45 A C ATOM 189 CG GLU A 130 67.799 11.117 126.464 1.00 36.20 A C ATOM 190 CD GLU A 130 69.207 10.871 126.996 1.00 37.68 A C ATOM 191 OE1 GLU A 130 69.330 10.501 128.182 1.00 43.10 A O ATOM 192 OE2 GLU A 130 70.189 11.031 126.237 1.00 32.89 A O ATOM 193 C GLU A 130 64.587 12.788 127.971 1.00 27.09 A C ATOM 194 O GLU A 130 64.154 12.167 128.939 1.00 29.20 A O ATOM 195 N ASP A 131 64.301 14.069 127.751 1.00 23.80 A N ATOM 196 CA ASP A 131 63.519 14.870 128.693 1.00 21.55 A C ATOM 197 GB ASP A 131 63.657 16.355 128.367 1.00 20.53 A C ATOM 198 CG ASP A 131 65.084 16.774 128.149 1.00 21.96 A C ATOM 199 OD1 ASP A 131 65.993 16.132 128.718 1.00 23.79 A O ATOM 200 OD2 ASP A 131 65.291 17.760 127.417 1.00 19.14 A O ATOM 201 C ASP A 131 62.029 14.589 128.821 1.00 22.60 A C ATOM 202 O ASP A 131 61.417 14.946 129.826 1.00 22.01 A O ATOM 203 N LEU A 132 61.426 13.985 127.808 1.00 21.60 A N ATOM 204 CA LEU A 132 59.996 13.736 127.862 1.00 17.46 A C ATOM 205 CB LEU A 132 59.274 14.744 126.964 1.00 18.77 A C ATOM 206 CO LEU A 132 59.410 16.228 127.329 1.00 16.38 A C ATOM 207 CD1 LEU A 132 58.952 17.103 126.185 1.00 16.14 A C ATOM 208 CD2 LEU A 132 58.584 16.513 128.574 1.00 17.73 A C ATOM 209 C LEU A 132 59.625 12.322 127.447 1.00 17.91 A C ATOM 210 O LEU A 132 60.350 11.668 126.703 1.00 20.57 A O ATOM 211 N PRO A 133 58.493 11.818 127.952 1.00 18.54 A N ATOM 212 CD PRO A 133 57.590 12.397 128.962 1.00 16.46 A C ATOM 213 CA PRO A 133 58.070 10.464 127.588 1.00 18.30 A C ATOM 214 CB PRO A 133 56.828 10.250 128.448 1.00 16.44 A C ATOM 215 CG PRO A 133 57.029 11.174 129.599 1.00 13.96 A C ATOM 216 C PRO A 133 57.739 10.482 126.092 1.00 18.28 A C ATOM 217 O PRO A 133 57.305 11.511 125.566 1.00 15.16 A O ATOM 218 N ARG A 134 57.931 9.358 125.412 1.00 18.49 A N ATOM 219 CA ARG A 134 57.661 9.313 123.978 1.00 20.66 A C ATOM 220 CB ARG A 134 58.084 7.961 123.411 1.00 20.98 A C ATOM 221 CG ARO A 134 59.563 7.723 123.628 1.00 21.85 A C ATOM 222 CD ARO A 134 60.064 6.476 122.953 1.00 25.93 A C ATOM 223 NE ARG A 134 61.506 6.346 123.137 1.00 29.18 A N ATOM 224 CZ ARG A 134 62.234 5.347 122.652 1.00 32.95 A C ATOM 225 NH1 ARG A 134 61.649 4.384 121.949 1.00 31.93 A N ATOM 226 NH2 ARG A 134 63.544 5.314 122.867 1.00 31.66 A N ATOM 227 C ARG A 134 56.217 9.633 123.615 1.00 20.30 A C ATOM 228 O ARG A 134 55.961 10.226 122.575 1.00 19.91 A O ATOM 229 N ALA A 135 55.274 9.256 124.470 1.00 19.00 A N ATOM 230 CA ALA A 135 53.871 9.552 124.201 1.00 20.03 A C ATOM 231 CB ALA A 135 52.980 8.861 125.237 1.00 18.70 A C ATOM 232 C ALA A 135 53.642 11.073 124.226 1.00 19.99 A C ATOM 233 O ALA A 135 52.814 11.601 123.489 1.00 19.37 A O ATOM 234 N VAL A 136 54.378 11.774 125.082 1.00 18.65 A N ATOM 235 CA VAL A 136 54.245 13.227 125.175 1.00 18.87 A C ATOM 236 CB VAL A 136 54.950 13.777 126.459 1.00 18.18 A C ATOM 237 CG1 VAL A 136 54.999 15.309 126.443 1.00 16.50 A C ATOM 238 CG2 VAL A 136 54.204 13.303 127.688 1.00 13.02 A C ATOM 239 C VAL A 136 54.838 13.900 123.930 1.00 17.85 A C ATOM 240 O VAL A 136 54.277 14.870 123.400 1.00 16.07 A O ATOM 241 N ILE A 137 55.969 13.374 123.469 1.00 14.93 A N ATOM 242 CA ILE A 137 56.630 13.916 122.295 1.00 13.94 A C ATOM 243 CB ILE A 137 58.035 13.292 122.121 1.00 13.55 A C ATOM 244 CG2 ILE A 137 58.657 13.730 120.789 1.00 10.34 A C ATOM 245 CG1 ILE A 137 58.917 13.705 123.307 1.00 11.84 A C ATOM 246 CD1 ILE A 137 60.329 13.165 123.274 1.00 8.78 A C ATOM 247 C ILE A 137 55.781 13.689 121.044 1.00 13.89 A C ATOM 248 O ILE A 137 55.557 14.616 120.270 1.00 13.43 A O ATOM 249 N ASP A 138 55.298 12.465 120.850 1.00 14.79 A N ATOM 250 CA ASP A 138 54.469 12.168 119.685 1.00 16.05 A C ATOM 251 CB ASP A 138 53.891 10.748 119.764 1.00 14.50 A C ATOM 252 CG ASP A 138 54.946 9.662 119.593 1.00 16.77 A C ATOM 253 OD1 ASP A 138 56.089 9.967 119.188 1.00 18.40 A O ATOM 254 OD2 ASP A 138 54.619 8.484 119.853 1.00 20.23 A O ATOM 255 C ASP A 138 53.317 13.170 119.602 1.00 16.70 A C ATOM 256 O ASP A 138 53.086 13.784 118.564 1.00 19.57 A O ATOM 257 N ASP A 139 52.612 13.337 120.716 1.00 16.62 A N ATOM 258 CA ASP A 139 51.460 14.232 120.801 1.00 15.09 A C ATOM 259 CB ASP A 139 50.812 14.099 122.181 1.00 14.62 A C ATOM 260 CG ASP A 139 49.611 15.003 122.354 1.00 16.52 A C ATOM 261 OD1 ASP A 139 48.584 14.769 121.692 1.00 19.96 A O ATOM 262 OD2 ASP A 139 49.688 15.953 123.152 1.00 12.35 A O ATOM 263 C ASP A 139 51.785 15.693 120.526 1.00 15.75 A C ATOM 264 O ASP A 139 51.004 16.396 119.894 1.00 17.52 A O ATOM 265 N ALA A 140 52.935 16.152 121.008 1.00 16.49 A N ATOM 266 CA ALA A 140 53.356 17.536 120.805 1.00 14.14 A C ATOM 267 CB ALA A 140 54.648 17.819 121.586 1.00 10.53 A C ATOM 268 C ALA A 140 53.576 17.805 119.319 1.00 13.23 A C ATOM 269 O ALA A 140 53.156 18.838 118.797 1.00 13.50 A O ATOM 270 N PHE A 141 54.249 16.877 118.645 1.00 12.36 A N ATOM 271 CA PHE A 141 54.501 17.017 117.216 1.00 15.20 A C ATOM 272 CB PHE A 141 55.431 15.901 116.722 1.00 13.79 A C ATOM 273 CG PHE A 141 56.867 16.073 117.146 1.00 11.40 A C ATOM 274 CD1 PHE A 141 57.408 17.340 117.318 1.00 12.07 A C ATOM 275 CD2 PHE A 141 57.685 14.973 117.341 1.00 11.50 A C ATOM 276 GE1 PHE A 141 58.752 17.507 117.678 1.00 15.23 A C ATOM 277 CE2 PHB A 141 59.032 15.133 117.701 1.00 10.84 A C ATOM 278 CZ PHB A 141 59.564 16.396 117.868 1.00 9.69 A C ATOM 279 C PHB A 141 53.183 16.988 116.433 1.00 15.88 A C ATOM 280 O PHE A 141 52.980 17.783 115.516 1.00 18.45 A O ATOM 281 N ALA A 142 52.289 16.080 116.815 1.00 15.46 A N ATOM 282 CA ALA A 142 50.997 15.940 116.156 1.00 16.51 A C ATOM 283 CB ALA A 142 50.235 14.769 116.751 1.00 16.42 A C ATOM 284 C ALA A 142 50.175 17.217 116.281 1.00 17.88 A C ATOM 285 O ALA A 142 49.519 17.642 115.327 1.00 14.95 A O ATOM 286 N ARG A 143 50.207 17.826 117.464 1.00 17.58 A N ATOM 287 CA ARG A 143 49.465 19.055 117.687 1.00 16.25 A C ATOM 288 CB ARG A 143 49.349 19.353 119.191 1.00 13.94 A C ATOM 289 CG ARG A 143 48.421 18.387 119.930 1.00 13.87 A C ATOM 290 CD ARG A 143 48.231 18.747 121.404 1.00 13.42 A C ATOM 291 NE ARG A 143 49.470 18.634 122.168 1.00 12.17 A N ATOM 292 CZ ARG A 143 50.164 19.671 122.631 1.00 14.73 A C ATOM 293 NH1 ARG A 143 49.732 20.910 122.416 1.00 12.72 A N ATOM 294 NH2 ARG A 143 51.305 19.471 123.287 1.00 14.62 A N ATOM 295 C ARG A 143 50.139 20.214 116.952 1.00 16.25 A C ATOM 296 O ARG A 143 49.478 21.162 116.535 1.00 18.41 A O ATOM 297 N ALA A 144 51.453 20.140 116.787 1.00 14.76 A N ATOM 298 CA ALA A 144 52.165 21.199 116.079 1.00 14.81 A C ATOM 299 CB ALA A 144 53.687 21.021 116.247 1.00 9.68 A C ATOM 300 C ALA A 144 51.763 21.169 114.592 1.00 15.68 A C ATOM 301 O ALA A 144 51.588 22.214 113.970 1.00 14.69 A O ATOM 302 N PHE A 145 51.605 19.968 114.033 1.00 16.80 A N ATOM 303 CA PHE A 145 51.193 19.815 112.632 1.00 17.22 A C ATOM 304 CB PHE A 145 51.386 18.367 112.154 1.00 14.07 A C ATOM 305 CG PHE A 145 52.791 18.045 111.744 1.00 9.59 A C ATOM 306 CD1 PHE A 145 53.433 18.797 110.767 1.00 10.98 A C ATOM 307 CD2 PHE A 145 53.472 16.990 112.326 1.00 9.63 A C ATOM 308 CE1 PEE A 145 54.739 18.503 110.373 1.00 10.38 A C ATOM 309 CE2 PHE A 145 54.781 16.687 111.939 1.00 11.84 A C ATOM 310 CZ PEE A 145 55.414 17.448 110.958 1.00 9.71 A C ATOM 311 C PEB A 145 49.729 20.209 112.438 1.00 19.32 A C ATOM 312 O PHE A 145 49.366 20.790 111.414 1.00 20.25 A O ATOM 313 N ALA A 146 48.889 19.891 113.420 1.00 18.99 A N ATOM 314 CA ALA A 146 47.471 20.224 113.330 1.00 20.15 A C ATOM 315 CB ALA A 146 46.730 19.695 114.542 1.00 16.75 A C ATOM 316 C ALA A 146 47.246 21.727 113.195 1.00 21.23 A C ATOM 317 O ALA A 146 46.272 22.153 112.592 1.00 24.43 A O ATOM 318 N LEU A 147 48.137 22.533 113.764 1.00 23.09 A N ATOM 319 CA LEU A 147 47.996 23.983 113.668 1.00 21.92 A C ATOM 320 CB LEU A 147 49.155 24.698 114.367 1.00 20.86 A C ATOM 321 CG LEU A 147 49.260 24.748 115.894 1.00 24.92 A C ATOM 322 CD1 LEU A 147 50.469 25.598 116.255 1.00 22.84 A C ATOM 323 CD2 LEU A 147 48.001 25.342 116.513 1.00 22.59 A C ATOM 324 C LEU A 147 47.984 24.422 112.206 1.00 22.21 A C ATOM 325 O LEU A 147 47.188 25.265 111.797 1.00 22.01 A O ATOM 326 N TRP A 148 48.884 23.842 111.425 1.00 21.86 A N ATOM 327 CA TRP A 148 49.013 24.196 110.026 1.00 23.11 A C ATOM 328 CB TRP A 148 50.413 23.831 109.534 1.00 19.89 A C ATOM 329 CG TRP A 148 51.513 24.569 110.249 1.00 21.33 A C ATOM 330 CD2 TRP A 148 51.827 25.964 110.138 1.00 21.93 A C ATOM 331 CE2 TRP A 148 52.965 26.203 110.942 1.00 20.27 A C ATOM 332 CE3 TRP A 148 51.259 27.036 109.435 1.00 18.40 A C ATOM 333 CD1 TRP A 148 52.445 24.037 111.100 1.00 20.02 A C ATOM 334 NE1 TRP A 148 53.320 25.012 111.517 1.00 17.63 A N ATOM 335 CZ2 TRP A 148 53.548 27.472 111.059 1.00 19.95 A C ATOM 336 CZ3 TRP A 148 51.838 28.297 109.553 1.00 19.74 A C ATOM 337 CH2 TRP A 148 52.972 28.503 110.359 1.00 18.39 A C ATOM 338 C TRP A 148 47.955 23.571 109.126 1.00 23.44 A C ATOM 339 O TRP A 148 47.419 24.237 108.244 1.00 21.73 A O ATOM 340 N SER A 149 47.645 22.300 109.351 1.00 25.55 A N ATOM 341 CA SER A 149 46.648 21.630 108.531 1.00 27.95 A C ATOM 342 CB SER A 149 46.618 20.127 108.823 1.00 28.12 A C ATOM 343 OG SER A 149 46.132 19.877 110.124 1.00 27.95 A O ATOM 344 C SER A 149 45.274 22.220 108.782 1.00 28.65 A C ATOM 345 O SER A 149 44.340 21.959 108.031 1.00 30.51 A O ATOM 346 N ALA A 150 45.148 23.022 109.833 1.00 27.46 A N ATOM 347 CA ALA A 150 43.864 23.627 110.151 1.00 27.51 A C ATOM 348 CB ALA A 150 43.817 24.013 111.620 1.00 24.47 A C ATOM 349 C ALA A 150 43.552 24.843 109.280 1.00 28.60 A C ATOM 350 O ALA A 150 42.393 25.187 109.091 1.00 28.82 A O ATOM 351 N VAL A 151 44.579 25.492 108.745 1.00 30.95 A N ATOM 352 CA VAL A 151 44.366 26.670 107.909 1.00 30.77 A C ATOM 353 CB VAL A 151 45.144 27.891 108.456 1.00 30.72 A C ATOM 354 CO1 VAL A 151 44.557 28.320 109.784 1.00 32.55 A C ATOM 355 CG2 VAL A 151 46.617 27.546 108.623 1.00 27.92 A C ATOM 356 C VAL A 151 44.765 26.451 106.455 1.00 30.85 A C ATOM 357 O VAL A 151 44.898 27.405 105.691 1.00 31.86 A O ATOM 358 N THR A 152 44.958 25.195 106.072 1.00 30.06 A N ATOM 359 CA THR A 152 45.339 24.879 104.703 1.00 30.51 A C ATOM 360 CB THR A 152 46.879 24.805 104.536 1.00 29.92 A C ATOM 361 OG1 THR A 152 47.390 23.686 105.273 1.00 28.72 A O ATOM 362 CG2 THR A 152 47.538 26.087 105.021 1.00 30.53 A C ATOM 363 C THR A 152 44.760 23.530 104.301 1.00 30.44 A C ATOM 364 O THR A 152 44.171 22.831 105.125 1.00 29.70 A O ATOM 365 N PRO A 153 44.904 23.157 103.017 1.00 30.47 A N ATOM 366 CD PRO A 153 45.298 24.023 101.887 1.00 30.45 A C ATOM 367 CA PRO A 153 44.392 21.875 102.527 1.00 30.14 A C ATOM 368 CB PRO A 153 44.174 22.145 101.042 1.00 30.77 A C ATOM 369 CG PRO A 153 45.304 23.059 100.717 1.00 32.01 A C ATOM 370 C PRO A 153 45.400 20.750 102.768 1.00 29.51 A C ATOM 371 O PRO A 153 45.190 19.619 102.336 1.00 30.25 A O ATOM 372 N LEU A 154 46.496 21.075 103.451 1.00 27.86 A N ATOM 373 CA LEU A 154 47.539 20.100 103.753 1.00 26.19 A C ATOM 374 CB LEU A 154 48.808 20.805 104.233 1.00 26.31 A C ATOM 375 CO LEU A 154 49.491 21.847 103.342 1.00 25.08 A C ATOM 376 CD1 LEU A 154 50.606 22.524 104.124 1.00 23.11 A C ATOM 377 CD2 LEU A 154 50.043 21.196 102.097 1.00 26.17 A C ATOM 378 C LEU A 154 47.104 19.116 104.832 1.00 25.56 A C ATOM 379 O LEU A 154 46.290 19.440 105.693 1.00 26.20 A O ATOM 380 N THR A 155 47.646 17.908 104.764 1.00 24.90 A N ATOM 381 CA THR A 155 47.363 16.875 105.752 1.00 26.31 A C ATOM 382 CB THR A 155 46.481 15.746 105.190 1.00 27.72 A C ATOM 383 OG1 THR A 155 47.094 15.203 104.014 1.00 32.34 A O ATOM 384 CG2 THR A 155 45.088 16.267 104.862 1.00 27.86 A C ATOM 385 C THR A 155 48.711 16.294 106.134 1.00 25.34 A C ATOM 386 O THR A 155 49.670 16.379 105.360 1.00 23.30 A O ATOM 387 N PHE A 156 48.790 15.707 107.323 1.00 23.87 A N ATOM 388 CA PHE A 156 50.044 15.139 107.787 1.00 22.82 A C ATOM 389 CB PHE A 156 50.630 16.046 108.870 1.00 19.73 A C ATOM 390 CG PHE A 156 50.935 17.434 108.375 1.00 15.72 A C ATOM 391 CD1 PHE A 156 52.108 17.693 107.676 1.00 15.50 A C ATOM 392 CD2 PHE A 156 50.011 18.461 108.536 1.00 16.19 A C ATOM 393 CE1 PHE A 156 52.357 18.952 107.139 1.00 14.40 A C ATOM 394 CE2 PHE A 156 50.249 19.725 108.004 1.00 15.79 A C ATOM 395 CZ PHE A 156 51.423 19.972 107.304 1.00 15.01 A C ATOM 396 C PHE A 156 49.864 13.718 108.286 1.00 24.14 A C ATOM 397 O PHE A 156 49.026 13.441 109.145 1.00 26.34 A O ATOM 398 N THR A 157 50.660 12.819 107.726 1.00 24.42 A N ATOM 399 CA THR A 157 50.595 11.410 108.070 1.00 23.69 A C ATOM 400 CB THR A 157 50.245 10.569 106.822 1.00 23.41 A C ATOM 401 OG1 THR A 157 48.935 10.931 106.373 1.00 25.91 A O ATOM 402 CG2 THR A 157 50.277 9.081 107.135 1.00 21.00 A C ATOM 403 C THR A 157 51.915 10.939 108.638 1.00 22.11 A C ATOM 404 O THR A 157 52.984 11.228 108.090 1.00 21.92 A O ATOM 405 N ARG A 158 51.830 10.214 109.745 1.00 22.59 A N ATOM 406 CA ARG A 158 53.015 9.679 110.394 1.00 22.35 A C ATOM 407 CB ARG A 158 52.780 9.534 111.899 1.00 21.18 A C ATOM 408 CG ARG A 158 53.998 9.010 112.630 1.00 21.22 A C ATOM 409 CD ARG A 158 53.758 8.843 114.113 1.00 20.30 A C ATOM 410 NE ARG A 158 54.959 8.340 114.776 1.00 20.99 A N ATOM 411 CZ ARG A 158 55.013 7.974 116.051 1.00 20.64 A C ATOM 412 NH1 ARG A 158 53.931 8.058 116.811 1.00 19.84 A N ATOM 413 NH2 ARG A 158 56.147 7.506 116.560 1.00 20.74 A N ATOM 414 C ARG A 158 53.362 8.320 109.802 1.00 21.92 A C ATOM 415 O ARG A 158 52.508 7.442 109.710 1.00 21.61 A O ATOM 416 N VAL A 159 54.618 8.156 109.399 1.00 24.22 A N ATOM 417 CA VAL A 159 55.092 6.901 108.823 1.00 25.52 A C ATOM 418 CB VAL A 159 55.403 7.059 107.311 1.00 23.23 A C ATOM 419 CO1 VAL A 159 54.147 7.523 106.573 1.00 19.77 A C ATOM 420 CG2 VAL A 159 56.539 8.045 107.109 1.00 21.91 A C ATOM 421 C VAL A 159 56.344 6.469 109.579 1.00 28.57 A C ATOM 422 O VAL A 159 56.842 7.212 110.424 1.00 29.72 A O ATOM 423 N TYR A 160 56.859 5.278 109.282 1.00 31.79 A N ATOM 424 CA TYR A 160 58.033 4.791 109.995 1.00 33.61 A C ATOM 425 CB TYR A 160 57.634 3.596 110.863 1.00 29.27 A C ATOM 426 CO TYR A 160 56.570 3.952 111.873 1.00 28.93 A C ATOM 427 CD1 TYR A 160 55.230 4.056 111.498 1.00 28.23 A C ATOM 428 CE2 TYR A 160 54.256 4.465 112.410 1.00 29.32 A C ATOM 429 CD2 TYR A 160 56.912 4.261 113.191 1.00 28.64 A C ATOM 430 CE2 TYR A 160 55.949 4.670 114.108 1.00 29.60 A C ATOM 431 CZ TYR A 160 54.626 4.772 113.712 1.00 30.04 A C ATOM 432 OH TYR A 160 53.680 5.193 114.616 1.00 32.56 A O ATOM 433 C TYR A 160 59.270 4.449 109.170 1.00 36.31 A C ATOM 434 O TYR A 160 60.097 3.640 109.591 1.00 39.18 A O ATOM 435 N SER A 161 59.414 5.075 108.010 1.00 37.86 A N ATOM 436 CA SER A 161 60.574 4.816 107.174 1.00 39.80 A C ATOM 437 CB SER A 161 60.166 4.018 105.933 1.00 38.63 A C ATOM 438 OG SER A 161 59.238 4.737 105.143 1.00 39.02 A O ATOM 439 C SER A 161 61.231 6.128 106.766 1.00 41.58 A C ATOM 440 O SER A 161 60.664 7.200 106.972 1.00 41.79 A O ATOM 441 N ARG A 162 62.426 6.033 106.187 1.00 44.11 A N ATOM 442 CA ARG A 162 63.188 7.198 105.739 1.00 46.57 A C ATOM 443 CB ARG A 162 64.613 6.790 105.350 1.00 48.67 A C ATOM 444 CG ARG A 162 65.408 6.045 106.418 1.00 53.36 A C ATOM 445 CD ARO A 162 64.757 4.721 106.797 1.00 57.23 A C ATOM 446 NE ARG A 162 65.661 3.839 107.528 1.00 60.31 A N ATOM 447 CZ ARG A 162 65.274 2.728 108.145 1.00 62.63 A C ATOM 448 NH1 ARG A 162 63.997 2.372 108.120 1.00 63.79 A N ATOM 449 NH2 ARG A 162 66.161 1.965 108.777 1.00 62.58 A N ATOM 450 C ARG A 162 62.537 7.862 104.529 1.00 47.42 A C ATOM 451 O ARG A 162 63.027 8.879 104.040 1.00 48.56 A O ATOM 452 N ASP A 163 61.441 7.282 104.048 1.00 48.01 A N ATOM 453 CA ASP A 163 60.739 7.804 102.876 1.00 46.94 A C ATOM 454 CB ASP A 163 59.909 6.695 102.227 1.00 52.93 A C ATOM 455 CG ASP A 163 60.766 5.584 101.665 1.00 56.71 A C ATOM 456 OD1 ASP A 163 61.681 5.891 100.871 1.00 59.29 A O ATOM 457 OD2 ASP A 163 60.525 4.409 102.013 1.00 61.03 A O ATOM 458 C ASP A 163 59.838 9.008 103.127 1.00 42.48 A C ATOM 459 O ASP A 163 59.350 9.627 102.181 1.00 43.42 A O ATOM 460 N ALA A 164 59.612 9.337 104.392 1.00 35.33 A N ATOM 461 CA ALA A 164 58.768 10.476 104.738 1.00 28.12 A C ATOM 462 CB ALA A 164 58.656 10.591 106.254 1.00 28.52 A C ATOM 463 C ALA A 164 59.332 11.776 104.159 1.00 24.32 A C ATOM 464 O ALA A 164 60.528 11.868 103.859 1.00 18.94 A O ATOM 465 N ASP A 165 58.468 12.776 103.996 1.00 20.55 A N ATOM 466 CA ASP A 165 58.910 14.070 103.491 1.00 19.96 A C ATOM 467 CB ASP A 165 57.732 14.931 103.033 1.00 20.58 A C ATOM 468 CG ASP A 165 56.953 14.302 101.918 1.00 19.34 A C ATOM 469 OD1 ASP A 165 57.577 13.931 100.907 1.00 22.92 A O ATOM 470 OD2 ASP A 165 55.720 14.185 102.053 1.00 20.26 A O ATOM 471 C ASP A 165 59.619 14.808 104.609 1.00 19.50 A C ATOM 472 O ASP A 165 60.669 15.387 104.403 1.00 20.89 A O ATOM 473 N ILE A 166 59.031 14.798 105.798 1.00 18.88 A N ATOM 474 CA ILE A 166 59.638 15.496 106.923 1.00 18.31 A C ATOM 475 CB ILE A 166 58.612 16.435 107.598 1.00 16.76 A C ATOM 476 CG2 ILE A 166 59.241 17.114 108.817 1.00 15.02 A C ATOM 477 CG1 ILE A 166 58.129 17.477 106.581 1.00 16.47 A C ATOM 478 CD1 ILE A 166 57.004 18.367 107.073 1.00 12.28 A C ATOM 479 C ILE A 166 60.198 14.523 107.950 1.00 18.31 A C ATOM 480 O ILE A 166 59.448 13.831 108.635 1.00 19.42 A O ATOM 481 N VAL A 167 61.522 14.453 108.032 1.00 16.42 A N ATOM 482 CA VAL A 167 62.172 13.577 108.992 1.00 14.89 A C ATOM 483 GB VAL A 167 63.410 12.891 108.391 1.00 16.42 A C ATOM 484 CO1 VAL A 167 64.133 12.076 109.464 1.00 14.30 A C ATOM 485 CG2 VAL A 167 62.984 11.982 107.243 1.00 18.08 A C ATOM 486 C VAL A 167 62.581 14.415 110.200 1.00 17.08 A C ATOM 487 O VAL A 167 63.232 15.456 110.064 1.00 13.46 A O ATOM 488 N ILE A 168 62.183 13.943 111.378 1.00 15.49 A N ATOM 489 CA ILE A 168 62.445 14.624 112.633 1.00 16.01 A C ATOM 490 CB ILE A 168 61.145 14.735 113.448 1.00 13.64 A C ATOM 491 CG2 ILE A 168 61.406 15.473 114.755 1.00 14.98 A C ATOM 492 CG1 ILE A 168 60.077 15.427 112.603 1.00 12.69 A C ATOM 493 CD1 ILE A 168 58.685 15.344 113.170 1.00 10.54 A C ATOM 494 C ILE A 168 63.482 13.906 113.486 1.00 16.29 A C ATOM 495 O ILE A 168 63.442 12.693 113.648 1.00 18.46 A O ATOM 496 N GLN A 169 64.414 14.656 114.045 1.00 19.10 A N ATOM 497 CA GLN A 169 65.407 14.028 114.890 1.00 20.39 A C ATOM 498 CB GLN A 169 66.536 13.443 114.043 1.00 23.58 A C ATOM 499 CG GLN A 169 67.428 14.481 113.409 1.00 28.43 A C ATOM 500 CD GLN A 169 68.723 13.890 112.901 1.00 32.40 A C ATOM 501 OE1 GLN A 169 69.551 13.411 113.678 1.00 36.26 A O ATOM 502 NE2 GLN A 169 68.908 13.917 111.591 1.00 33.78 A N ATOM 503 C GLN A 169 65.998 14.991 115.905 1.00 19.32 A C ATOM 504 O GLN A 169 66.009 16.206 115.694 1.00 17.87 A O ATOM 505 N PHE A 170 66.482 14.423 117.005 1.00 15.27 A N ATOM 506 CA PHE A 170 67.124 15.180 118.062 1.00 16.05 A C ATOM 507 CB PHE A 170 66.613 14.740 119.444 1.00 13.11 A C ATOM 508 CG PHE A 170 65.164 15.056 119.690 1.00 11.58 A C ATOM 509 CD1 PHE A 170 64.157 14.272 119.131 1.00 9.60 A C ATOM 510 CD2 PHE A 170 64.807 16.148 120.475 1.00 11.94 A C ATOM 511 CE1 PHE A 170 62.817 14.572 119.352 1.00 10.10 A C ATOM 512 CE2 PHE A 170 63.466 16.458 120.701 1.00 11.51 A C ATOM 513 CZ PHE A 170 62.471 15.671 120.141 1.00 11.15 A C ATOM 514 C PHE A 170 68.611 14.873 117.953 1.00 17.13 A C ATOM 515 O PHE A 170 68.998 13.728 117.747 1.00 18.15 A O ATOM 516 N GLY A 171 69.450 15.889 118.082 1.00 17.88 A N ATOM 517 CA GLY A 271 70.879 15.655 118.006 1.00 19.53 A C ATOM 518 C GLY A 171 71.642 16.630 118.878 1.00 21.64 A C ATOM 519 O GLY A 171 71.083 17.631 119.324 1.00 22.76 A O ATOM 520 N VAL A 172 72.912 16.332 119.138 1.00 23.09 A N ATOM 521 CA VAL A 172 73.756 17.205 119.950 1.00 25.50 A C ATOM 522 CB VAL A 172 74.109 16.560 121.326 1.00 26.03 A C ATOM 523 CG1 VAL A 172 72.844 16.252 122.083 1.00 26.98 A C ATOM 524 CG2 VAL A 172 74.918 15.292 121.134 1.00 25.99 A C ATOM 525 C VAL A 172 75.038 17.489 119.174 1.00 26.07 A C ATOM 526 O VAL A 172 75.653 16.574 118.615 1.00 24.44 A O ATOM 527 N ALA A 173 75.427 18.760 119.139 1.00 27.68 A N ATOM 528 CA ALA A 173 76.618 19.184 118.411 1.00 28.80 A C ATOM 529 CB ALA A 173 77.868 18.664 119.111 1.00 29.58 A C ATOM 530 C ALA A 173 76.548 18.659 116.974 1.00 29.57 A C ATOM 531 O ALA A 173 75.538 18.843 116.289 1.00 27.64 A U ATOM 532 N GLU A 174 77.619 18.006 116.530 1.00 29.27 A N ATOM 533 CA GLU A 174 77.699 17.437 115.189 1.00 32.29 A C ATOM 534 CB GLU A 174 79.078 16.815 114.972 1.00 41.88 A C ATOM 535 CG GLU A 174 80.209 17.511 115.722 1.00 51.63 A C ATOM 536 CD GLU A 174 80.512 18.892 115.178 1.00 57.77 A C ATOM 537 OE1 GLU A 174 81.379 19.584 115.757 1.00 58.88 A O ATOM 538 OE2 GLU A 174 79.888 19.284 114.167 1.00 62.24 A C ATOM 539 C GLU A 174 76.657 16.340 115.076 1.00 30.20 A C ATOM 540 O GLU A 174 76.668 15.409 115.874 1.00 31.68 A O ATOM 541 N HIS A 175 75.768 16.418 114.092 1.00 27.49 A N ATOM 542 CA HIS A 175 74.748 15.385 113.979 1.00 27.72 A C ATOM 543 CB HIS A 175 73.473 15.827 114.688 1.00 24.97 A C ATOM 544 CG HIS A 175 72.928 17.118 114.175 1.00 20.26 A C ATOM 545 CD2 HIS A 175 72.023 17.379 113.203 1.00 17.16 A C ATOM 546 ND1 HIS A 175 73.354 18.341 114.644 1.00 20.15 A N ATOM 547 GE1 HIS A 175 72.734 19.302 113.982 1.00 18.26 A C ATOM 548 NE2 HIS A 175 71.922 18.744 113.102 1.00 15.77 A N ATOM 549 C HIS A 175 74.392 14.949 112.571 1.00 30.79 A C ATOM 550 O HIS A 175 73.257 14.536 112.317 1.00 32.24 A C ATOM 551 N GLY A 176 75.341 15.042 111.647 1.00 32.67 A N ATOM 552 CA GLY A 176 75.048 14.601 110.297 1.00 34.93 A C ATOM 553 C GLY A 176 75.221 15.634 109.213 1.00 36.14 A C ATOM 554 O GLY A 176 76.066 15.481 108.340 1.00 37.19 A O ATOM 555 N ASP A 177 74.399 16.674 109.240 1.00 37.27 A N ATOM 556 CA ASP A 177 74.512 17.721 108.242 1.00 35.71 A C ATOM 557 CB ASP A 177 73.267 18.600 108.231 1.00 34.06 A C ATOM 558 CG ASP A 177 72.828 19.006 109.617 1.00 32.01 A C ATOM 559 OD1 ASP A 177 73.684 19.394 110.439 1.00 28.22 A O ATOM 560 OD2 ASP A 177 71.613 18.942 109.872 1.00 33.33 A O ATOM 561 C ASP A 177 75.734 18.551 108.587 1.00 36.61 A C ATOM 562 O ASP A 177 76.570 18.132 109.389 1.00 40.71 A O ATOM 563 N GLY A 178 75.845 19.730 107.996 1.00 34.57 A N ATOM 564 CA GLY A 178 77.008 20.546 108.278 1.00 36.70 A C ATOM 565 C GLY A 178 76.753 21.721 109.194 1.00 36.80 A C ATOM 566 O GLY A 178 77.520 22.684 109.184 1.00 37.18 A O ATOM 567 N TYR A 179 75.688 21.649 109.991 1.00 37.02 A N ATOM 568 CA TYR A 179 75.344 22.731 110.908 1.00 34.28 A C ATOM 569 CB TYR A 179 74.078 23.436 110.425 1.00 36.20 A C ATOM 570 CG TYR A 179 74.181 23.932 109.003 1.00 42.47 A C ATOM 571 CD1 TYR A 179 73.949 23.076 107.927 1.00 45.68 A C ATOM 572 CE1 TYR A 179 74.065 23.524 106.609 1.00 46.33 A C ATOM 573 CD2 TYR A 179 74.536 25.253 108.728 1.00 44.79 A C ATOM 574 CE2 TYR A 179 74.658 25.712 107.415 1.00 45.00 A C ATOM 575 CZ TYR A 179 74.420 24.843 106.362 1.00 47.34 A C ATOM 576 OH TYR A 179 74.528 25.293 105.062 1.00 48.94 A O ATOM 577 C TYR A 179 75.153 22.235 112.335 1.00 31.65 A C ATOM 578 O TYR A 179 74.033 22.165 112.838 1.00 29.30 A O ATOM 579 N PRO A 180 76.260 21.895 113.014 1.00 31.79 A N ATOM 580 CD PRO A 180 77.653 22.113 112.589 1.00 30.47 A C ATOM 581 CA PRO A 180 76.212 21.401 114.394 1.00 30.83 A C ATOM 582 CB PRO A 180 77.685 21.194 114.739 1.00 31.29 A C ATOM 583 CG PRO A 180 78.370 22.238 113.916 1.00 31.47 A C ATOM 584 C PRO A 180 75.532 22.381 115.335 1.00 28.21 A C ATOM 585 O PRO A 180 75.505 23.579 115.073 1.00 28.60 A O ATOM 586 N PHE A 181 74.971 21.866 116.422 1.00 25.93 A N ATOM 587 CA PHE A 181 74.306 22.721 117.388 1.00 26.27 A C ATOM 588 CB PHE A 181 73.238 21.937 118.158 1.00 23.67 A C ATOM 589 CG PHE A 181 72.012 21.625 117.346 1.00 21.97 A C ATOM 590 CD1 PHE A 181 71.262 22.649 116.778 1.00 22.39 A C ATOM 591 CD2 PHE A 181 71.590 20.309 117.165 1.00 21.41 A C ATOM 592 CE1 PHE A 181 70.102 22.369 116.040 1.00 22.23 A C ATOM 593 CE2 PHE A 181 70.432 20.019 116.430 1.00 20.84 A C ATOM 594 CZ PHE A 181 69.688 21.052 115.868 1.00 19.15 A C ATOM 595 C PHE A 181 75.351 23.306 118.335 1.00 28.41 A C ATOM 596 O PHE A 181 76.498 22.863 118.354 1.00 27.60 A O ATOM 597 N ASP A 182 74.943 24.290 119.127 1.00 28.53 A N ATOM 598 CA ASP A 182 75.848 24.979 120.031 1.00 29.79 A C ATOM 599 CB ASP A 182 75.723 26.478 119.769 1.00 28.81 A C ATOM 600 CG ASP A 182 74.284 26.937 119.799 1.00 29.97 A C ATOM 601 OD1 ASP A 182 73.464 26.193 120.358 1.00 30.97 A O ATOM 602 OD2 ASP A 182 73.962 28.025 119.284 1.00 31.92 A O ATOM 603 C ASP A 182 75.677 24.718 121.535 1.00 31.81 A C ATOM 604 O ASP A 182 75.941 25.608 122.346 1.00 34.01 A O ATOM 605 N GLY A 183 75.249 23.520 121.921 1.00 31.93 A N ATOM 606 CA GLY A 183 75.085 23.236 123.341 1.00 31.05 A C ATOM 607 C GLY A 183 73.943 24.014 123.976 1.00 32.23 A C ATOM 608 O GLY A 183 73.094 24.524 123.276 1.00 32.15 A O ATOM 609 N LYS A 184 73.923 24.122 125.299 1.00 32.11 A N ATOM 610 CA LYS A 184 72.851 24.832 126.002 1.00 33.02 A C ATOM 611 CB LYS A 184 73.209 24.984 127.484 1.00 37.17 A C ATOM 612 CG LYS A 184 72.020 25.232 128.396 1.00 41.04 A C ATOM 613 CD LYS A 184 71.101 24.017 128.419 1.00 44.80 A C ATOM 614 CE LYS A 184 69.925 24.219 129.353 1.00 45.32 A C ATOM 615 NZ LYS A 184 70.371 24.435 130.752 1.00 48.28 A N ATOM 616 C LYS A 184 72.539 26.207 125.424 1.00 31.99 A C ATOM 617 O LYS A 184 73.445 26.975 125.118 1.00 34.08 A O ATOM 618 N ASP A 185 71.250 26.504 125.278 1.00 30.60 A N ATOM 619 CA ASP A 185 70.777 27.787 124.756 1.00 29.01 A C ATOM 620 CB ASP A 185 71.068 28.895 125.763 1.00 33.03 A C ATOM 621 CG ASP A 185 70.304 28.712 127.046 1.00 36.57 A C ATOM 622 OD1 ASP A 185 69.058 28.796 127.011 1.00 39.21 A O ATOM 623 OD2 ASP A 185 70.947 28.470 128.090 1.00 40.55 A O ATOM 624 C ASP A 185 71.311 28.198 123.394 1.00 26.92 A C ATOM 625 O ASP A 185 71.999 27.438 122.727 1.00 25.74 A O ATOM 626 N GLY A 186 70.992 29.422 122.990 1.00 24.58 A N ATOM 627 CA GLY A 186 71.431 29.904 121.695 1.00 26.41 A C ATOM 628 C GLY A 186 70.472 29.395 120.637 1.00 26.21 A C ATOM 629 O GLY A 186 69.280 29.693 120.691 1.00 27.15 A O ATOM 630 N LEU A 187 70.987 28.625 119.684 1.00 26.00 A N ATOM 631 CA LEU A 187 70.166 28.058 118.622 1.00 25.00 A C ATOM 632 CB LEU A 187 71.057 27.560 117.483 1.00 25.51 A C ATOM 633 CG LEU A 187 70.323 27.068 116.233 1.00 31.44 A C ATOM 634 CD1 LEU A 187 69.618 28.248 115.564 1.00 27.44 A C ATOM 635 CD2 LEU A 187 71.313 26.409 115.271 1.00 32.87 A C ATOM 636 C LEU A 187 69.394 26.885 119.220 1.00 24.47 A C ATOM 637 O LEU A 187 69.996 25.979 119.775 1.00 23.75 A O ATOM 638 N LEU A 188 68.071 26.881 119.097 1.00 22.38 A N ATOM 639 CA LEU A 188 67.272 25.800 119.673 1.00 20.10 A C ATOM 640 CB LEU A 188 65.930 26.349 120.158 1.00 17.21 A C ATOM 641 CG LEU A 188 65.981 27.580 121.077 1.00 19.72 A C ATOM 642 CD1 LEU A 188 64.565 27.997 121.447 1.00 14.44 A C ATOM 643 CD2 LEU A 188 66.791 27.275 122.329 1.00 16.62 A C ATOM 644 C LEU A 188 67.026 24.638 118.712 1.00 21.08 A C ATOM 645 O LEU A 188 66.907 23.477 119.129 1.00 18.95 A O ATOM 646 N ALA A 189 66.956 24.958 117.426 1.00 19.08 A N ATOM 647 CA ALA A 189 66.703 23.963 116.400 1.00 16.54 A C ATOM 648 CB ALA A 189 65.297 23.398 116.575 1.00 16.25 A C ATOM 649 C ALA A 189 66.824 24.626 115.039 1.00 17.08 A C ATOM 650 O ALA A 189 67.110 25.815 114.943 1.00 16.33 A O ATOM 651 N HIS A 190 66.627 23.842 113.988 1.00 16.66 A N ATOM 652 CA HIS A 190 66.656 24.361 112.636 1.00 18.31 A C ATOM 653 CB HIS A 190 68.099 24.705 112.191 1.00 18.50 A C ATOM 654 CG His A 190 69.055 23.550 112.164 1.00 17.26 A C ATOM 655 CD2 HIS A 190 68.920 22.281 111.712 1.00 20.42 A C ATOM 656 ND1 HIS A 190 70.369 23.671 112.567 1.00 18.18 A N ATOM 657 CE1 HIS A 190 71.002 22.531 112.365 1.00 17.27 A C ATOM 658 NE2 HIS A 190 70.145 21.671 111.846 1.00 18.89 A N ATOM 659 C HIS A 190 65.982 23.372 111.699 1.00 18.42 A C ATOM 660 O HIS A 190 65.985 22.168 111.956 1.00 18.06 A O ATOM 661 N ALA A 191 65.367 23.887 110.637 1.00 19.52 A N ATOM 662 CA ALA A 191 64.672 23.049 109.659 1.00 20.18 A C ATOM 663 CB ALA A 191 63.163 23.158 109.853 1.00 17.02 A C ATOM 664 C ALA A 191 65.052 23.460 108.242 1.00 2~.20 A C ATOM 665 O ALA A 191 65.547 24.563 108.026 1.00 22.82 A O ATOM 666 N PUB A 192 64.822 22.569 107.279 1.00 24.96 A N ATOM 667 CA PHE A 192 65.156 22.847 105.884 1.00 24.10 A C ATOM 668 CB PHE A 192 66.013 21.724 105.303 1.00 24.41 A C ATOM 669 CG PHE A 192 67.299 21.491 106.042 1.00 25.34 A C ATOM 670 CD1 PHE A 192 67.328 20.696 107.184 1.00 27.98 A C ATOM 671 CD2 PHE A 192 68.483 22.059 105.594 1.00 26.82 A C ATOM 672 CE1 PHE A 192 68.524 20.466 107.870 1.00 27.32 A C ATOM 673 CE2 PHE A 192 69.682 21.839 106.267 1.00 27.38 A C ATOM 674 CZ PHE A 192 69.703 21.039 107.410 1.00 28.50 A C ATOM 675 C PHE A 192 63.906 23.012 105.033 1.00 25.05 A C ATOM 676 O PHE A 192 62.891 22.346 105.270 1.00 24.67 A O ATOM 677 N PRO A 193 63.967 23.908 104.027 1.00 25.22 A N ATOM 678 CD PRO A 193 65.156 24.708 103.684 1.00 25.93 A C ATOM 679 CA PRO A 193 62.861 24.203 103.103 1.00 24.58 A C ATOM 680 CB PRO A 193 63.434 25.292 102.195 1.00 22.65 A C ATOM 681 CG PRO A 193 64.542 25.894 102.997 1.00 26.18 A C ATOM 682 C PRO A 193 62.454 22.970 102.299 1.00 24.59 A C ATOM 683 O PRO A 193 63.231 22.018 102.164 1.00 23.68 A O ATOM 684 N PRO A 194 61.233 22.981 101.745 1.00 23.30 A N ATOM 685 CD PRO A 194 60.243 24.072 101.820 1.00 20.97 A C ATOM 686 CA PRO A 194 60.718 21.861 100.949 1.00 24.06 A C ATOM 687 CB PRO A 194 59.445 22.441 100.334 1.00 22.11 A C ATOM 688 CG PRO A 194 58.968 23.371 101.408 1.00 21.80 A C ATOM 689 C PRO A 194 61.710 21.371 99.891 1.00 23.68 A C ATOM 690 O PRO A 194 62.473 22.147 99.325 1.00 21.32 A O ATOM 691 N GLY A 195 61.688 20.071 99.631 1.00 26.27 A N ATOM 692 CA GLY A 195 62.584 19.500 98.645 1.00 26.15 A C ATOM 693 C OLY A 195 62.908 18.059 98.978 1.00 28.20 A C ATOM 694 O GLY A 195 62.355 17.505 99.926 1.00 29.23 A O ATOM 695 N PRO A 196 63.801 17.420 98.211 1.00 28.08 A N ATOM 696 CD PRO A 196 64.340 17.902 96.926 1.00 26.14 A C ATOM 697 CA PRO A 196 64.188 16.025 98.445 1.00 28.94 A C ATOM 698 CB PRO A 196 64.613 15.563 97.057 1.00 27.73 A C ATOM 699 CG PRO A 196 65.288 16.788 96.526 1.00 26.49 A C ATOM 700 C PRO A 196 65.320 15.876 99.472 1.00 29.39 A C ATOM 701 O PRO A 196 65.972 16.855 99.837 1.00 31.26 A O ATOM 702 N GLY A 197 65.542 14.646 99.930 1.00 28.16 A N ATOM 703 CA GLY A 197 66.605 14.374 100.884 1.00 26.43 A C ATOM 704 C GLY A 197 66.466 15.066 102.223 1.00 25.89 A C ATOM 705 O GLY A 197 65.399 15.077 102.803 1.00 26.43 A O ATOM 706 N ILE A 198 67.548 15.648 102.719 1.00 24.59 A N ATOM 707 CA ILE A 198 67.515 16.336 104.000 1.00 27.36 A C ATOM 708 CB ILE A 198 68.929 16.809 104.385 1.00 29.59 A C ATOM 709 CG2 ILE A 198 69.376 17.929 103.447 1.00 29.40 A C ATOM 710 CG1 ILE A 198 68.946 17.268 105.840 1.00 30.60 A C ATOM 711 CD1 ILE A 198 70.323 17.634 106.334 1.00 33.20 A C ATOM 712 C ILE A 198 66.558 17.537 103.966 1.00 29.10 A C ATOM 713 O ILB A 198 66.139 18.048 105.009 1.00 28.33 A O ATOM 714 N GLN A 199 66.212 17.975 102.760 1.00 27.92 A N ATOM 715 CA OLN A 199 65.304 19.100 102.578 1.00 28.08 A C ATOM 716 CB GLN A 199 65.103 19.366 101.081 1.00 31.22 A C ATOM 717 CG GLN A 199 65.534 20.754 100.637 1.00 40.25 A C ATOM 718 CD GLN A 199 66.996 21.044 100.939 1.00 42.74 A C ATOM 719 OE1 GLN A 199 67.459 22.173 100.787 1.00 45.88 A O ATOM 720 NE2 GLN A 199 67.730 20.022 101.362 1.00 44.96 A N ATOM 721 C GLN A 199 63.967 18.794 103.241 1.00 23.32 A C ATOM 722 O GLN A 199 63.442 17.705 103.097 1.00 20.60 A O ATOM 723 N GLY A 200 63.416 19.759 103.967 1.00 23.07 A N ATOM 724 CA GLY A 200 62.147 19.537 104.637 1.00 19.23 A C ATOM 725 C GLY A 200 62.279 18.891 106.009 1.00 18.68 A C ATOM 726 O GLY A 200 61.283 18.719 106.708 1.00 22.62 A O ATOM 727 N ASP A 201 63.496 18.532 106.405 1.00 17.22 A N ATOM 728 CA ASP A 201 63.712 17.903 107.711 1.00 18.97 A C ATOM 729 CB ASP A 201 64.974 17.038 107.687 1.00 16.29 A C ATOM 730 CG ASP A 201 64.834 15.835 106.774 1.00 18.51 A C ATOM 731 OD1 ASP A 201 63.724 15.612 106.260 1.00 15.25 A O ATOM 732 OD2 ASP A 201 65.824 15.104 106.576 1.00 19.34 A O ATOM 733 C ASP A 201 63.813 18.920 108.844 1.00 19.43 A C ATOM 734 O ASP A 201 64.156 20.076 108.621 1.00 21.36 A O ATOM 735 N ALA A 202 63.513 18.476 110.062 1.00 19.70 A N ATOM 736 CA ALA A 202 63.559 19.341 111.239 1.00 18.01 A C ATOM 737 CB ALA A 202 62.142 19.616 111.729 1.00 17.65 A C ATOM 738 C ALA A 202 64.389 18.706 112.350 1.00 18.31 A C ATOM 739 O ALA A 202 64.107 17.588 112.790 1.00 17.93 A O ATOM 740 N HIS A 203 65.407 19.431 112.805 1.00 17.90 A N ATOM 741 CA HIS A 203 66.304 18.945 113.847 1.00 17.65 A C ATOM 742 CB HIS A 203 67.736 18.938 113.313 1.00 15.54 A C ATOM 743 CG HIS A 203 67.906 18.147 112.053 1.00 16.78 A C ATOM 744 CD2 HIS A 203 67.100 17.239 111.453 1.00 14.93 A C ATOM 745 ND1 HIS A 203 69.025 18.248 111.258 1.00 15.86 A N ATOM 746 CE1 HIS A 203 68.902 17.439 110.221 1.00 16.22 A C ATOM 747 NE2 HIS A 203 67.742 16.816 110.316 1.00 14.71 A N ATOM 748 C HIS A 203 66.241 19.782 115.123 1.00 17.94 A C ATOM 749 O HIS A 203 66.248 21.008 115.063 1.00 17.49 A O ATOM 750 N PHE A 204 66.193 19.115 116.275 1.00 17.60 A N ATOM 751 CA PHE A 204 66.133 19.814 117.559 1.00 17.27 A C ATOM 752 CB PHE A 204 64.884 19.389 118.342 1.00 15.27 A C ATOM 753 CO PHE A 204 63.602 19.576 117.579 1.00 15.59 A C ATOM 754 CD1 PHE A 204 63.234 18.678 116.581 1.00 15.30 A C ATOM 755 CD2 PHE A 204 62.790 20.683 117.816 1.00 15.08 A C ATOM 756 CE1 PHR A 204 62.075 18.882 115.826 1.00 17.01 A C ATOM 757 CE2 PHE A 204 61.636 20.899 117.071 1.00 14.70 A C ATOM 758 CZ PHE A 204 61.275 19.998 116.073 1.00 16.71 A C ATOM 759 C PHE A 204 67.378 19.555 118.402 1.00 17.45 A C ATOM 760 O PHE A 204 67.834 18.414 118.510 1.00 15.59 A O ATOM 761 N ASP A 205 67.928 20.619 118.987 1.00 16.31 A N ATOM 762 CA ASP A 205 69.109 20.503 119.837 1.00 16.90 A C ATOM 763 CB ASP A 205 69.729 21.876 120.082 1.00 17.51 A C ATOM 764 CG ASP A 205 71.037 21.788 120.840 1.00 18.97 A C ATOM 765 OD1 ASP A 205 71.305 20.732 121.441 1.00 18.91 A O ATOM 766 OD2 ASP A 205 71.798 22.767 120.836 1.00 18.05 A O ATOM 767 C ASP A 205 68.730 19.883 121.185 1.00 17.81 A C ATOM 768 O ASP A 205 68.024 20.498 121.988 1.00 18.19 A O ATOM 769 N ASP A 206 69.208 18.670 121.436 1.00 19.02 A N ATOM 770 CA ASP A 206 68.880 17.994 122.676 1.00 20.78 A C ATOM 771 CB ASP A 206 68.881 16.473 122.468 1.00 22.45 A C ATOM 772 CG ASP A 206 68.015 15.737 123.497 1.00 25.21 A C ATOM 773 OD1 ASP A 206 67.013 16.317 123.968 1.00 26.38 A O ATOM 774 OD2 ASP A 206 68.321 14.574 123.822 1.00 24.25 A O ATOM 775 C ASP A 206 69.781 18.386 123.847 1.00 21.59 A C ATOM 776 O ASP A 206 69.827 17.692 124.849 1.00 23.96 A O ATOM 777 N ASP A 207 70.513 19.488 123.715 1.00 23.27 A N ATOM 778 CA ASP A 207 71.331 19.969 124.823 1.00 22.12 A C ATOM 779 CB ASP A 207 72.605 20.664 124.342 1.00 23.08 A C ATOM 780 CG ASP A 207 73.809 19.738 124.348 1.00 24.02 A C ATOM 781 OD1 ASP A 207 73.806 18.762 125.124 1.00 26.09 A O ATOM 782 OD2 ASP A 207 74.766 19.989 123.591 1.00 23.97 A O ATOM 783 C ASP A 207 70.458 20.966 125.570 1.00 21.36 A C ATOM 784 O ASP A 207 70.817 21.459 126.634 1.00 22.22 A O ATOM 785 N GLU A 208 69.303 21.255 124.982 1.00 20.40 A N ATOM 786 CA GLU A 208 68.341 22.172 125.567 1.00 21.00 A C ATOM 787 GB GLU A 208 67.477 22.810 124.475 1.00 22.83 A C ATOM 788 CG GLU A 208 68.262 23.464 123.363 1.00 27.27 A C ATOM 789 CD GLU A 208 68.931 24.732 123.805 1.00 29.69 A C ATOM 790 OE1 GLU A 208 69.277 24.846 124.996 1.00 36.53 A O ATOM 791 OE2 GLU A 208 69.119 25.620 122.959 1.00 34.99 A O ATOM 792 C GLU A 208 67.446 21.345 126.464 1.00 19.62 A C ATOM 793 O GLU A 208 67.323 20.140 126.271 1.00 18.21 A O ATOM 794 N LEU A 209 66.831 21.990 127.447 1.00 18.09 A N ATOM 795 CA LEU A 209 65.898 21.311 128.331 1.00 17.54 A C ATOM 796 GB LBU A 209 65.887 21.982 129.710 1.00 15.57 A C ATOM 797 CG LEU A 209 64.850 21.473 130.714 1.00 19.72 A C ATOM 798 CD1 LEU A 209 65.072 20.004 130.986 1.00 18.15 A C ATOM 799 CD2 LEU A 209 64.947 22.273 132.008 1.00 18.92 A C ATOM 800 C LEU A 209 64.529 21.445 127.653 1.00 16.85 A C ATOM 801 O LEU A 209 64.001 22.549 127.519 1.00 18.96 A O ATOM 802 N TRP A 210 63.974 20.328 127.197 1.00 15.69 A N ATOM 803 CA TRP A 210 62.678 20.347 126.531 1.00 14.68 A C ATOM 804 CB TRP A 210 62.628 19.319 125.384 1.00 12.69 A C ATOM 805 CG TRP A 210 63.520 19.686 124.252 1.00 14.19 A C ATOM 806 CD2 TRP A 210 63.396 20.834 123.402 1.00 14.74 A C ATOM 807 CE2 TRP A 210 64.531 20.855 122.562 1.00 13.82 A C ATOM 808 CE3 TRP A 210 62.438 21.850 123.273 1.00 13.00 A C ATOM 809 CD1 TRP A 210 64.688 19.072 123.893 1.00 15.08 A C ATOM 810 NE1 TRP A 210 65.302 19.770 122.885 1.00 15.30 A N ATOM 811 CZ2 TRP A 210 64.736 21.854 121.605 1.00 12.58 A C ATOM 812 CZ3 TRP A 210 62.646 22.845 122.319 1.00 11.89 A C ATOM 813 CH2 TRP A 210 63.787 22.837 121.499 1.00 10.54 A C ATOM 814 C TRP A 210 61.549 20.080 127.503 1.00 14.10 A C ATOM 815 O TRP A 210 61.614 19.147 128.301 1.00 12.40 A O ATOM 816 N SER A 211 60.504 20.897 127.406 1.00 13.94 A N ATOM 817 CA SER A 211 59.347 20.791 128.272 1.00 13.15 A C ATOM 818 GB SER A 211 59.568 21.682 129.492 1.00 14.15 A C ATOM 819 OG SER A 211 58.635 21.392 130.505 1.00 17.46 A O ATOM 820 C SER A 211 58.102 21.243 127.505 1.00 15.84 A C ATOM 821 O SER A 211 58.080 21.195 126.280 1.00 17.08 A O ATOM 822 N LEU A 212 57.068 21.667 128.233 1.00 15.21 A N ATOM 823 CA LEU A 212 55.819 22.160 127.645 1.00 13.96 A C ATOM 824 CB LEU A 212 54.836 21.018 127.391 1.00 10.99 A C ATOM 825 CO LEU A 212 55.168 19.921 126.378 1.00 11.66 A C ATOM 826 CD1 LEU A 212 54.139 18.817 126.510 1.00 8.67 A C ATOM 827 CD2 LEU A 212 55.202 20.494 124.967 1.00 7.27 A C ATOM 828 C LEU A 212 55.180 23.125 128.635 1.00 17.00 A C ATOM 829 O LEU A 212 55.367 22.992 129.837 1.00 19.75 A O ATOM 830 N GLY A 213 54.421 24.088 128.132 1.00 19.26 A N ATOM 831 CA GLY A 213 53.748 25.037 129.003 1.00 20.32 A C ATOM 832 C GLY A 213 54.639 26.040 129.713 1.00 19.73 A C ATOM 833 O GLY A 213 55.759 26.294 129.285 1.00 20.34 A O ATOM 834 N LYS A 214 54.123 26.618 130.795 1.00 20.81 A N ATOM 835 CA LYS A 214 54.861 27.597 131.588 1.00 21.44 A C ATOM 836 CB LYS A 214 53.909 28.339 132.537 1.00 23.26 A C ATOM 837 CG LYS A 214 52.925 29.266 131.838 1.00 25.72 A C ATOM 838 CD LYS A 214 51.935 29.898 132.805 1.00 27.35 A C ATOM 839 CE LYS A 214 51.002 28.859 133.402 1.00 30.75 A C ATOM 840 NZ LYS A 214 49.866 29.485 134.138 1.00 35.19 A N ATOM 841 C LYS A 214 55.917 26.863 132.398 1.00 21.38 A C ATOM 842 O LYS A 214 55.743 25.688 132.729 1.00 22.09 A O ATOM 843 N GLY A 215 57.008 27.548 132.721 1.00 19.58 A N ATOM 844 CA GLY A 215 58.061 26.911 133.491 1.00 20.65 A C ATOM 845 C GLY A 215 59.403 27.007 132.798 1.00 20.80 A C ATOM 846 O GLY A 215 59.496 27.528 131.689 1.00 20.47 A O ATOM 847 N GLN A 391 60.449 26.500 133.439 1.00 21.31 A N ATOM 848 CA GLN A 391 61.779 26.564 132.848 1.00 22.25 A C ATOM 849 CB GLN A 391 62.851 26.279 133.917 1.00 26.72 A C ATOM 850 CG GLN A 391 63.213 24.832 134.110 1.00 34.22 A C ATOM 851 CD GLN A 391 62.000 23.953 134.238 1.00 41.18 A C ATOM 852 OE1 OLN A 391 61.117 24.211 135.054 1.00 48.75 A O ATOM 853 NE2 GLN A 391 61.944 22.903 133.427 1.00 46.74 A N ATOM 854 C GLN A 391 61.886 25.585 131.676 1.00 20.85 A C ATOM 855 O GLN A 391 61.097 24.654 131.561 1.00 20.10 A O ATOM 856 N GLY A 392 62.866 25.794 130.808 1.00 19.12 A N ATOM 857 CA GLY A 392 63.005 24.931 129.653 1.00 20.95 A C ATOM 858 C GLY A 392 62.266 25.565 128.487 1.00 19.62 A C ATOM 859 O GLY A 392 61.669 26.627 128.637 1.00 17.25 A O ATOM 860 N TYR A 393 62.301 24.921 127.328 1.00 19.08 A N ATOM 861 CA TYR A 393 61.637 25.454 126.141 1.00 17.64 A C ATOM 862 CB TYR A 393 62.646 25.560 125.000 1.00 18.65 A C ATOM 863 CO TYR A 393 63.773 26.534 125.256 1.00 18.22 A C ATOM 864 CD1 TYR A 393 63.586 27.905 125.079 1.00 19.12 A C ATOM 865 CE1 TYR A 393 64.626 28.807 125.291 1.00 20.27 A C ATOM 866 CD2 TYR A 393 65.036 26.084 125.660 1.00 18.43 A C ATOM 867 CE2 TYR A 393 66.091 26.980 125.878 1.00 18.43 A C ATOM 868 CZ TYR A 393 65.879 28.339 125.691 1.00 20.99 A C ATOM 869 OH TYR A 393 66.911 29.229 125.892 1.00 18.81 A O ATOM 870 C TYR A 393 60.474 24.563 125.714 1.00 16.46 A C ATOM 871 O TYR A 393 60.552 23.343 125.812 1.00 18.48 A O ATOM 872 N SER A 394 59.393 25.165 125.238 1.00 16.19 A N ATOM 873 CA SER A 394 58.248 24.376 124.799 1.00 16.88 A C ATOM 874 CB SER A 394 57.026 25.268 124.581 1.00 15.95 A C ATOM 875 OG SER A 394 55.900 24.491 124.195 1.00 16.81 A O ATOM 876 C SER A 394 58.555 23.638 123.501 1.00 16.05 A C ATOM 877 O SER A 394 58.781 24.262 122.468 1.00 17.59 A O ATOM 878 N LEU A 395 58.563 22.311 123.557 1.00 13.28 A N ATOM 879 CA LEU A 395 58.825 21.508 122.373 1.00 13.52 A C ATOM 880 CB LEU A 395 58.874 20.022 122.734 1.00 9.81 A C ATOM 881 CG LEU A 395 59.158 19.078 121.559 1.00 10.42 A C ATOM 882 CD1 LEU A 395 60.518 19.417 120.974 1.00 8.66 A C ATOM 883 CD2 LEU A 395 59.117 17.618 122.012 1.00 7.01 A C ATOM 884 C LEU A 395 57.720 21.758 121.345 1.00 13.87 A C ATOM 885 O LEU A 395 57.979 21.792 120.149 1.00 15.88 A O ATOM 886 N PHE A 396 56.495 21.936 121.836 1.00 13.30 A N ATOM 887 CA PHE A 396 55.319 22.195 121.010 1.00 13.78 A C ATOM 888 CB PHE A 396 54.069 22.270 121.907 1.00 14.03 A C ATOM 889 CG PHE A 396 52.850 22.840 121.225 1.00 15.47 A C ATOM 890 CD1 PHE A 396 52.243 22.168 120.167 1.00 16.74 A C ATOM 891 CD2 PHE A 396 52.322 24.064 121.632 1.00 16.39 A C ATOM 892 CE1 PHE A 396 51.128 22.706 119.518 1.00 15.98 A C ATOM 893 CE2 PHE A 396 51.211 24.611 120.993 1.00 17.97 A C ATOM 894 CZ PHE A 396 50.611 23.929 119.929 1.00 16.67 A C ATOM 895 C PHE A 396 55.440 23.476 120.178 1.00 15.62 A C ATOM 896 O PHE A 396 55.242 23.455 118.958 1.00 15.38 A O ATOM 897 N LEU A 397 55.756 24.587 120.837 1.00 14.66 A N ATOM 898 CA LEU A 397 55.892 25.861 120.148 1.00 14.57 A C ATOM 899 CB LEU A 397 55.998 27.009 121.155 1.00 16.23 A C ATOM 900 CG LEU A 397 54.739 27.366 121.951 1.00 19.61 A C ATOM 901 CD1 LEU A 397 55.033 28.532 122.908 1.00 17.04 A C ATOM 902 CD2 LEU A 397 53.615 27.734 120.982 1.00 18.70 A C ATOM 903 C LEU A 397 57.084 25.912 119.202 1.00 16.31 A C ATOM 904 O LEU A 397 57.002 26.511 118.132 1.00 18.67 A O ATOM 905 N VAL A 398 58.198 25.299 119.591 1.00 17.18 A N ATOM 906 CA VAL A 398 59.379 25.309 118.738 1.00 16.87 A C ATOM 907 GB VAL A 398 60.643 24.855 119.513 1.00 15.03 A C ATOM 908 CG1 VAL A 398 61.838 24.750 118.562 1.00 7.55 A C ATOM 909 CG2 VAL A 398 60.953 25.867 120.636 1.00 13.62 A C ATOM 910 C VAL A 398 59.157 24.410 117.524 1.00 17.35 A C ATOM 911 O VAL A 398 59.610 24.715 116.427 1.00 16.12 A O ATOM 912 N ALA A 399 58.446 23.307 117.725 1.00 17.18 A N ATOM 913 CA ALA A 399 58.159 22.386 116.629 1.00 18.10 A C ATOM 914 CB ALA A 399 57.440 21.146 117.155 1.00 17.14 A C ATOM 915 C ALA A 399 57.296 23.084 115.583 1.00 16.31 A C ATOM 916 O ALA A 399 57.540 22.962 114.387 1.00 17.90 A O ATOM 917 N ALA A 400 56.288 23.814 116.048 1.00 16.32 A N ATOM 918 CA ALA A 400 55.385 24.531 115.161 1.00 16.53 A C ATOM 919 CB ALA A 400 54.340 25.283 115.970 1.00 11.88 A C ATOM 920 C ALA A 400 56.162 25.495 114.278 1.00 17.89 A C ATOM 921 O ALA A 400 55.859 25.640 113.101 1.00 18.21 A O ATOM 922 N HIS A 401 57.169 26.142 114.858 1.00 18.94 A N ATOM 923 CA HIS A 401 58.009 27.094 114.140 1.00 16.00 A C ATOM 924 CB HIS A 401 58.934 27.812 115.123 1.00 15.08 A C ATOM 925 CG HIS A 401 59.800 28.858 114.490 1.00 16.12 A C ATOM 926 CD2 HIS A 401 61.049 28.788 113.972 1.00 11.82 A C ATOM 927 ND1 HIS A 401 59.400 30.169 114.344 1.00 16.08 A N ATOM 928 CE1 HIS A 401 60.367 30.860 113.767 1.00 16.27 A C ATOM 929 NE2 HIS A 401 61.377 30.045 113.531 1.00 10.47 A N ATOM 930 C HIS A 401 58.849 26.371 113.091 1.00 17.48 A C ATOM 931 O HIS A 401 58.899 26.785 111.939 1.00 17.04 A O ATOM 932 N GLU A 402 59.512 25.292 113.497 1.00 16.98 A N ATOM 933 CA GLU A 402 60.346 24.523 112.583 1.00 19.94 A C ATOM 934 CB GLU A 402 61.058 23.374 113.311 1.00 20.34 A C ATOM 935 CG GLU A 402 62.029 23.804 114.410 1.00 20.68 A C ATOM 936 CD GLU A 402 62.758 25.100 114.095 1.00 17.45 A C ATOM 937 CE1 GLU A 402 63.300 25.234 112.987 1.00 18.70 A O ATOM 938 CE2 GLU A 402 62.793 25.984 114.967 1.00 17.38 A O ATOM 939 C GLU A 402 59.522 23.952 111.432 1.00 20.70 A C ATOM 940 O GLU A 402 59.961 23.972 110.285 1.00 20.70 A 0 ATOM 941 N PHE A 403 58.336 23.437 111.735 1.00 20.02 A N ATOM 942 CA PHE A 403 57.482 22.889 110.691 1.00 20.64 A C ATOM 943 CB PHE A 403 56.262 22.184 111.293 1.00 20.51 A C ATOM 944 CG PHE A 403 56.608 21.005 112.173 1.00 20.43 A C ATOM 945 CD1 PHE A 403 57.865 20.398 112.094 1.00 17.64 A C ATOM 946 CD2 PHE A 403 55.678 20.509 113.087 1.00 14.31 A C ATOM 947 CE1 PHE A 403 58.192 19.319 112.916 1.00 18.71 A C ATOM 948 CE2 PRE A 403 55.988 19.424 113.918 1.00 12.75 A C ATOM 949 CZ PHE A 403 57.243 18.826 113.838 1.00 15.90 A C ATOM 950 C PHE A 403 57.040 23.998 109.732 1.00 20.93 A C ATOM 951 O PHE A 403 56.699 23.728 108.587 1.00 20.08 A O ATOM 952 N GLY A 404 57.041 25.241 110.208 1.00 20.24 A N ATOM 953 CA GLY A 404 56.685 26.355 109.352 1.00 18.45 A C ATOM 954 C GLY A 404 57.748 26.442 108.263 1.00 19.06 A C ATOM 955 O GLY A 404 57.438 26.584 107.082 1.00 18.85 A O ATOM 956 N HIS A 405 59.011 26.353 108.666 1.00 17.32 A N ATOM 957 CA HIS A 405 60.119 26.382 107.718 1.00 18.09 A C ATOM 958 CB HIS A 405 61.460 26.317 108.446 1.00 15.13 A C ATOM 959 CG HIS A 405 61.859 27.600 109.095 1.00 19.30 A C ATOM 960 CD2 HIS A 405 62.362 27.859 110.323 1.00 15.40 A C ATOM 961 ND1 HIS A 405 61.769 28.816 108.452 1.00 18.08 A N ATOM 962 CE1 HIS A 405 62.197 29.769 109.258 1.00 17.34 A C ATOM 963 NE2 HIS A 405 62.563 29.214 110.399 1.00 18.40 A N ATOM 964 C HIS A 405 60.040 25.195 106.761 1.00 18.79 A C ATOM 965 O HIS A 405 60.171 25.352 105.554 1.00 22.20 A O ATOM 966 N ALA A 406 59.838 24.007 107.320 1.00 18.37 A N ATOM 967 CA ALA A 406 59.754 22.780 106.545 1.00 17.99 A C ATOM 968 CB ALA A 406 59.511 21.606 107.484 1.00 15.77 A C ATOM 969 C ALA A 406 58.665 22.838 105.468 1.00 17.88 A C ATOM 970 O ALA A 406 58.673 22.045 104.535 1.00 15.94 A O ATOM 971 N LEU A 407 57.730 23.773 105.612 1.00 20.32 A N ATOM 972 CA LEU A 407 56.646 23.935 104.647 1.00 22.45 A C ATOM 973 CB LEU A 407 55.307 24.158 105.367 1.00 21.52 A C ATOM 974 CG LEU A 407 54.789 23.030 106.266 1.00 22.77 A C ATOM 975 CD1 LEU A 407 53.461 23.421 106.888 1.00 19.54 A C ATOM 976 CD2 LEU A 407 54.629 21.766 105.447 1.00 25.90 A C ATOM 977 C LEU A 407 56.921 25.103 103.694 1.00 23.47 A C ATOM 978 O LEU A 407 56.093 25.422 102.844 1.00 23.57 A O ATOM 979 N GLY A 408 58.077 25.743 103.852 1.00 22.90 A N ATOM 980 CA GLY A 408 58.444 26.847 102.983 1.00 23.36 A C ATOM 981 C GLY A 408 58.411 28.268 103.528 1.00 24.25 A C ATOM 982 O GLY A 408 58.891 29.190 102.868 1.00 22.84 A O ATOM 983 N LEU A 409 57.855 28.463 104.719 1.00 25.11 A N ATOM 984 CA LEU A 409 57.777 29.804 105.290 1.00 24.70 A C ATOM 985 CB LEU A 409 56.853 29.828 106.508 1.00 22.64 A C ATOM 986 CG LEU A 409 55.352 29.682 106.281 1.00 25.21 A C ATOM 987 CD1 LEU A 409 54.639 29.943 107.588 1.00 21.69 A C ATOM 988 CD2 LEU A 409 54.880 30.664 105.212 1.00 24.00 A C ATOM 989 C LEU A 409 59.123 30.347 105.711 1.00 25.87 A C ATOM 990 O LEU A 409 59.989 29.598 106.156 1.00 26.76 A O ATOM 991 N ASP A 410 59.294 31.656 105.558 1.00 27.29 A N ATOM 992 CA ASP A 410 60.517 32.323 105.980 1.00 29.12 A C ATOM 993 CB ASP A 410 60.990 33.338 104.933 1.00 34.79 A C ATOM 994 CG ASP A 410 61.553 32.678 103.687 1.00 42.97 A C ATOM 995 OD1 ASP A 410 62.184 31.602 103.799 1.00 48.11 A O ATOM 996 OD2 ASP A 410 61.381 33.247 102.590 1.00 47.38 A O ATOM 997 C ASP A 410 60.188 33.050 107.289 1.00 27.33 A C ATOM 998 O ASP A 410 59.046 33.026 107.751 1.00 19.85 A O ATOM 999 N HIS A 411 61.190 33.687 107.883 1.00 25.92 A N ATOM 1000 CA HIS A 411 60.995 34.418 109.128 1.00 27.93 A C ATOM 1001 CB HIS A 411 62.345 34.843 109.699 1.00 25.18 A C ATOM 1002 CG HIS A 411 63.056 33.747 110.430 1.00 25.67 A C ATOM 1003 CD2 HIS A 411 62.579 32.692 111.134 1.00 22.64 A C ATOM 1004 ND1 HIS A 411 64.429 33.660 110.493 1.00 24.52 A N ATOM 1005 CE1 HIS A 411 64.768 32.596 111.199 1.00 24.55 A C ATOM 1006 NE2 HIS A 411 63.664 31.992 111.598 1.00 21.02 A N ATOM 1007 C HIS A 411 60.103 35.634 108.947 1.00 28.39 A C ATOM 1008 O HIS A 411 60.096 36.257 107.890 1.00 27.54 A O ATOM 1009 N SER A 412 59.348 35.953 109.992 1.00 28.70 A N ATOM 1010 CA SER A 412 58.441 37.090 109.989 1.00 28.94 A C ATOM 1011 CB SER A 412 57.139 36.716 110.696 1.00 27.79 A C ATOM 1012 CG SER A 412 56.288 37.836 110.831 1.00 28.82 A O ATOM 1013 C SER A 412 59.090 38.264 110.708 1.00 30.69 A C ATOM 1014 O SER A 412 60.020 38.081 111.489 1.00 31.96 A O ATOM 1015 N SER A 413 58.601 39.468 110.437 1.00 30.98 A N ATOM 1016 CA SER A 413 59.132 40.664 111.075 1.00 33.39 A C ATOM 1017 CB SER A 413 59.334 41.775 110.039 1.00 34.31 A C ATOM 1018 CG SER A 413 58.154 42.003 109.294 1.00 35.39 A O ATOM 1019 C SER A 413 58.175 41.125 112.166 1.00 32.91 A C ATOM 1020 O SER A 413 58.454 42.076 112.893 1.00 35.58 A O ATOM 1021 N VAL A 414 57.043 40.436 112.264 1.00 31.58 A N ATOM 1022 CA VAL A 414 56.023 40.725 113.264 1.00 31.56 A C ATOM 1023 GB VAL A 414 54.637 40.234 112.792 1.00 31.76 A C ATOM 1024 CG1 VAL A 414 53.578 40.582 113.816 1.00 31.52 A C ATOM 1025 CG2 VAL A 414 54.304 40.849 111.455 1.00 30.36 A C ATOM 1026 C VAL A 414 56.399 40.007 114.564 1.00 31.65 A C ATOM 1027 O VAL A 414 56.415 38.778 114.630 1.00 30.34 A O ATOM 1028 N PRO A 415 56.696 40.775 115.620 1.00 31.44 A N ATOM 1029 CD PRO A 415 56.730 42.248 115.656 1.00 29.01 A C ATOM 1030 CA PRO A 415 57.080 40.220 116.920 1.00 28.81 A C ATOM 1031 CB PRO A 415 57.116 41.461 117.802 1.00 29.03 A C ATOM 1032 CG PRO A 415 57.628 42.513 116.837 1.00 27.34 A C ATOM 1033 C PRO A 415 56.156 39.157 117.503 1.00 26.99 A C ATOM 1034 O PRO A 415 56.626 38.199 118.098 1.00 26.82 A O ATOM 1035 N GLU A 416 54.849 39.316 117.336 1.00 28.55 A N ATOM 1036 CA GLU A 416 53.907 38.343 117.881 1.00 29.16 A C ATOM 1037 CB GLU A 416 52.597 39.029 118.276 1.00 33.01 A C ATOM 1038 CG GLU A 416 52.180 40.147 117.341 1.00 42.66 A C ATOM 1039 CD GLU A 416 52.947 41.437 117.590 1.00 43.72 A C ATOM 1040 OE1 GLU A 416 53.148 42.204 116.626 1.00 43.99 A O ATOM 1041 OE2 GLU A 416 53.336 41.690 118.752 1.00 46.02 A O ATOM 1042 C GLU A 416 53.612 37.163 116.957 1.00 28.85 A C ATOM 1043 O GLU A 416 52.820 36.289 117.297 1.00 30.41 A O ATOM 1044 N ALA A 417 54.257 37.125 115.798 1.00 26.45 A N ATOM 1045 CA ALA A 417 54.037 36.029 114.867 1.00 24.95 A C ATOM 1046 CB ALA A 417 54.429 36.452 113.456 1.00 23.05 A C ATOM 1047 C ALA A 417 54.868 34.826 115.303 1.00 24.52 A C ATOM 1048 O ALA A 417 55.952 34.986 115.861 1.00 23.59 A O ATOM 1049 N LEU A 418 54.354 33.625 115.049 1.00 22.60 A N ATOM 1050 CA LEU A 418 55.060 32.399 115.396 1.00 21.25 A C ATOM 1051 CB LEU A 418 54.186 31.183 115.084 1.00 24.09 A C ATOM 1052 CG LEU A 418 54.819 29.794 115.255 1.00 25.61 A C ATOM 1053 CD1 LEU A 418 55.205 29.584 116.704 1.00 24.01 A C ATOM 1054 CD2 LEU A 418 53.851 28.711 114.802 1.00 24.22 A C ATOM 1055 C LEU A 418 56.378 32.281 114.639 1.00 20.33 A C ATOM 1056 O LEU A 418 57.336 31.699 115.139 1.00 17.86 A O ATOM 1057 N MET A 419 56.425 32.836 113.431 1.00 20.15 A N ATOM 1058 CA MET A 419 57.632 32.763 112.620 1.00 20.11 A C ATOM 1059 CB MET A 419 57.286 32.817 111.130 1.00 19.41 A C ATOM 1060 CG MET A 419 56.562 31.575 110.616 1.00 18.20 A C ATOM 1061 SD MET A 419 57.267 29.973 111.160 1.00 18.41 A S ATOM 1062 CE MET A 419 58.852 29.969 110.370 1.00 13.77 A C ATOM 1063 C MET A 419 58.678 33.816 112.953 1.00 20.18 A C ATOM 1064 O MET A 419 59.679 33.946 112.256 1.00 20.02 A O ATOM 1065 N TYR A 420 58.450 34.571 114.022 1.00 22.13 A N ATOM 1066 CA TYR A 420 59.433 35.561 114.443 1.00 23.96 A C ATOM 1067 CB TYR A 420 58.921 36.336 115.653 1.00 28.74 A C ATOM 1068 CG TYR A 420 59.721 37.578 115.957 1.00 33.66 A C ATOM 1069 CD1 TYR A 420 59.747 38.654 115.064 1.00 35.38 A C ATOM 1070 GE1 TYR A 420 60.495 39.791 115.334 1.00 36.85 A C ATOM 1071 CD2 TYR A 420 60.464 37.674 117.128 1.00 35.51 A C ATOM 1072 CE2 TYR A 420 61.215 38.804 117.409 1.00 38.35 A C ATOM 1073 CZ TYR A 420 61.228 39.858 116.512 1.00 40.13 A C ATOM 1074 OH TYR A 420 61.973 40.976 116.801 1.00 41.02 A O ATOM 1075 C TYR A 420 60.679 34.746 114.812 1.00 22.16 A C ATOM 1076 O TYR A 420 60.583 33.744 115.515 1.00 20.07 A O ATOM 1077 N PRO A 421 61.863 35.172 114.347 1.00 23.33 A N ATOM 1078 CD PRO A 421 62.072 36.447 113.634 1.00 24.71 A C ATOM 1079 CA PRO A 421 63.148 34.501 114.591 1.00 24.11 A C ATOM 1080 CB PRO A 421 64.129 35.342 113.773 1.00 24.83 A C ATOM 1081 CG PRO A 421 63.542 36.703 113.850 1.00 23.46 A C ATOM 1082 C PRO A 421 63.624 34.301 116.028 1.00 24.67 A C ATOM 1083 O PRO A 421 64.649 33.659 116.258 1.00 23.19 A O ATOM 1084 N MET A 422 62.870 34.827 116.986 1.00 23.77 A N ATOM 1085 CA MET A 422 63.228 34.732 118.393 1.00 24.04 A C ATOM 1086 CB MET A 422 63.351 36.148 118.961 1.00 29.95 A C ATOM 1087 CG MET A 422 63.671 36.231 120.433 1.00 39.49 A C ATOM 1088 SD MET A 422 63.479 37.927 121.034 1.00 49.06 A S ATOM 1089 CE MET A 422 61.893 37.842 121.866 1.00 39.08 A C ATOM 1090 C MET A 422 62.181 33.938 119.171 1.00 22.85 A C ATOM 1091 O MET A 422 60.983 34.062 118.915 1.00 21.77 A O ATOM 1092 N TYR A 423 62.626 33.117 120.114 1.00 19.77 A N ATOM 1093 CA TYR A 423 61.699 32.324 120.913 1.00 21.78 A C ATOM 1094 CB TYR A 423 62.441 31.214 121.659 1.00 19.09 A C ATOM 1095 CG TYR A 423 61.551 30.425 122.599 1.00 18.13 A C ATOM 1096 GD1 TYR A 423 60.797 29.344 122.139 1.00 18.66 A C ATOM 1097 CE1 TYR A 423 59.962 28.623 122.996 1.00 16.35 A C ATOM 1098 CD2 TYR A 423 61.445 30.769 123.946 1.00 17.67 A C ATOM 1099 CE2 TYR A 423 60.612 30.059 124.811 1.00 17.18 A C ATOM 1100 CZ TYR A 423 59.874 28.987 124.330 1.00 19.92 A C ATOM 1101 OH TYR A 423 59.053 28.278 125.182 1.00 18.58 A O ATOM 1102 C TYR A 423 60.964 33.168 121.950 1.00 23.28 A C ATOM 1103 O TYR A 423 61.568 34.001 122.616 1.00 23.95 A O ATOM 1104 N ARG A 424 59.662 32.942 122.087 1.00 25.46 A N ATOM 1105 CA ARG A 424 58.869 33.651 123.084 1.00 31.01 A C ATOM 1106 CB ARG A 424 58.376 35.005 122.550 1.00 35.79 A C ATOM 1107 CO ARG A 424 57.230 34.932 121.573 1.00 43.60 A C ATOM 1108 CD ARG A 424 56.693 36.313 121.235 1.00 50.63 A C ATOM 1109 NE ARG A 424 55.481 36.228 120.420 1.00 58.11 A N ATOM 1110 CZ ARG A 424 54.340 35.676 120.828 1.00 62.35 A C ATOM 1111 NH1 ARG A 424 54.247 35.158 122.049 1.00 65.08 A N ATOM 1112 NH2 ARG A 424 53.291 35.634 120.015 1.00 62.97 A N ATOM 1113 C ARG A 424 57.690 32.777 123.499 1.00 29.80 A C ATOM 1114 O ARG A 424 56.830 32.450 122.691 1.00 29.90 A O ATOM 1115 N PHE A 425 57.654 32.374 124.762 1.00 29.63 A N ATOM 1116 CA PHE A 425 56.555 31.534 125.203 1.00 28.26 A C ATOM 1117 CB PHE A 425 56.807 30.963 126.596 1.00 24.65 A C ATOM 1118 CG PHE A 425 55.660 30.152 127.112 1.00 23.69 A G ATOM 1119 CD1 PHE A 425 54.673 30.740 127.898 1.00 22.35 A C ATOM 1120 CD2 PHE A 425 55.506 28.820 126.729 1.00 21.86 A C ATOM 1121 CE1 PHE A 425 53.542 30.016 128.288 1.00 23.01 A C ATOM 1122 CE2 PHE A 425 54.379 28.086 127.113 1.00 21.25 A C ATOM 1123 CZ PHE A 425 53.395 28.684 127.892 1.00 21.91 A C ATOM 1124 C PHE A 425 55.236 32.287 125.205 1.00 29.92 A C ATOM 1125 O PHE A 425 55.177 33.475 125.525 1.00 32.27 A O ATOM 1126 N THR A 426 54.172 31.586 124.843 1.00 28.15 A N ATOM 1127 CA THR A 426 52.858 32.195 124.817 1.00 28.89 A C ATOM 1128 CB THR A 426 52.581 32.896 123.463 1.00 30.65 A C ATOM 1129 OG1 THR A 426 51.258 33.445 123.476 1.00 30.50 A O ATOM 1130 CG2 THR A 426 52.692 31.913 122.309 1.00 27.51 A C ATOM 1131 C THR A 426 51.771 31.168 125.054 1.00 28.39 A C ATOM 1132 O THR A 426 51.936 29.991 124.763 1.00 27.43 A O ATOM 1133 N GLU A 427 50.662 31.627 125.615 1.00 31.92 A N ATOM 1134 CA GLU A 427 49.515 30.767 125.864 1.00 33.81 A C ATOM 1135 CB GLU A 427 48.931 31.032 127.252 1.00 35.60 A C ATOM 1136 CG GLU A 427 49.820 30.574 128.402 1.00 41.56 A C ATOM 1137 CD GLU A 427 49.178 30.786 129.765 1.00 43.70 A C ATOM 1138 OE1 GLU A 427 48.985 31.959 130.162 1.00 45.79 A O ATOM 1139 OE2 GLU A 427 48.865 29.779 130.437 1.00 43.08 A O ATOM 1140 C GLU A 427 48.501 31.133 124.785 1.00 33.55 A C ATOM 1141 O GLU A 427 48.634 32.165 124.127 1.00 32.48 A O ATOM 1142 N GLY A 428 47.492 30.297 124.596 1.00 32.38 A N ATOM 1143 CA GLY A 428 46.509 30.596 123.575 1.00 34.96 A C ATOM 1144 C GLY A 428 47.015 30.234 122.189 1.00 35.38 A C ATOM 1145 O GLY A 428 48.137 29.740 122.050 1.00 34.55 A O ATOM 1146 N PRO A 429 46.210 30.482 121.139 1.00 35.27 A N ATOM 1147 CD PRO A 429 44.979 31.286 121.203 1.00 35.48 A C ATOM 1148 CA PRO A 429 46.555 30.185 119.744 1.00 32.90 A C ATOM 1149 CB PRO A 429 45.396 30.803 118.966 1.00 33.89 A C ATOM 1150 CO PRO A 429 44.964 31.931 119.848 1.00 34.64 A C ATOM 1151 C PRO A 429 47.913 30.740 119.329 1.00 30.15 A C ATOM 1152 O PRO A 429 48.156 31.939 119.403 1.00 32.20 A O ATOM 1153 N PRO A 430 48.817 29.858 118.886 1.00 27.85 A N ATOM 1154 CD PRO A 430 48.637 28.397 118.903 1.00 26.06 A C ATOM 1155 CA PRO A 430 50.173 30.211 118.450 1.00 27.78 A C ATOM 1156 CB PRO A 430 50.869 28.849 118.335 1.00 28.30 A C ATOM 1157 CG PRO A 430 50.029 27.927 119.193 1.00 29.20 A C ATOM 1158 C PRO A 430 50.260 30.989 117.135 1.00 27.63 A C ATOM 1159 O PRO A 43O 51.068 31.909 117.000 1.00 26.32 A O ATOM 1160 N LEU A 431 49.437 30.611 116.164 1.00 26.85 A N ATOM 1161 CA LEU A 431 49.470 31.257 114.858 1.00 28.30 A C ATOM 1162 CB LEU A 431 48.752 30.395 113.815 1.00 26.29 A C ATOM 1163 CG LEU A 431 49.353 29.024 113.507 1.00 26.78 A C ATOM 1164 CD1 LEU A 431 48.615 28.430 112.326 1.00 27.79 A C ATOM 1165 CD2 LEU A 431 50.827 29.144 113.188 1.00 25.85 A C ATOM 1166 C LEU A 431 48.897 32.658 114.815 1.00 26.95 A C ATOM 1167 O LEU A 431 47.776 32.891 115.248 1.00 27.17 A O ATOM 1168 N HIS A 432 49.681 33.585 114.279 1.00 27.31 A N ATOM 1169 CA HIS A 432 49.262 34.971 114.144 1.00 29.66 A C ATOM 1170 CB HIS A 432 50.469 35.883 114.367 1.00 30.80 A C ATOM 1171 CO HIS A 432 50.157 37.342 114.263 1.00 35.25 A C ATOM 1172 CD2 HIS A 432 50.006 38.291 115.216 1.00 36.05 A C ATOM 1173 ND1 HIS A 432 49.973 37.980 113.056 1.00 35.61 A N ATOM 1174 CE1 HIS A 432 49.724 39.260 113.269 1.00 35.01 A C ATOM 1175 NE2 HIS A 432 49.739 39.474 114.571 1.00 37.63 A N ATOM 1176 C H1S A 432 48.688 35.148 112.729 1.00 31.08 A C ATOM 1177 O HIS A 432 48.989 34.353 111.843 1.00 31.29 A O ATOM 1178 N LYS A 433 47.855 36.169 112.525 1.00 30.77 A N ATOM 1179 CA LYS A 433 47.252 36.437 111.214 1.00 31.04 A C ATOM 1180 GB LYS A 433 46.590 37.817 111.186 1.00 36.69 A C ATOM 1181 CG LYS A 433 45.486 38.010 112.205 1.00 46.32 A C ATOM 1182 CD LYS A 433 45.180 39.489 112.428 1.00 52.39 A C ATOM 1183 CE LYS A 433 44.194 39.680 113.585 1.00 57.26 A C ATOM 1184 NZ LYS A 433 43.913 41.116 113.889 1.00 59.05 A N ATOM 1185 C LYS A 433 48.328 36.411 110.148 1.00 30.86 A C ATOM 1186 O LYS A 433 48.111 35.954 109.025 1.00 28.27 A O ATOM 1187 N ASP A 434 49.496 36.919 110.511 1.00 29.06 A N ATOM 1188 CA ASP A 434 50.609 36.960 109.591 1.00 26.69 A C ATOM 1189 CB ASP A 434 51.766 37.732 110.213 1.00 26.22 A C ATOM 1190 CG ASP A 434 52.923 37.905 109.258 1.00 27.32 A C ATOM 1191 OD1 ASP A 434 53.916 37.168 109.388 1.00 27.96 A O ATOM 1192 OD2 ASP A 434 52.837 38.774 108.366 1.00 29.60 A O ATOM 1193 C ASP A 434 51.052 35.557 109.202 1.00 27.04 A C ATOM 1194 O ASP A 434 51.350 35.300 108.039 1.00 26.95 A O ATOM 1195 N ASP A 435 51.086 34.644 110.169 1.00 26.04 A N ATOM 1196 CA ASP A 435 51.496 33.270 109.890 1.00 26.18 A C ATOM 1197 CB ASP A 435 51.629 32.453 111.186 1.00 25.76 A C ATOM 1198 CG ASP A 435 52.659 33.026 112.159 1.00 23.37 A C ATOM 1199 OD1 ASP A 43S 53.833 33.231 111.778 1.00 17.56 A O ATOM 1200 OD2 ASP A 435 52.281 33.257 113.319 1.00 21.37 A O ATOM 1201 C ASP A 435 50.483 32.586 108.979 1.00 26.53 A C ATOM 1202 O ASP A 435 50.857 31.854 108.065 1.00 27.59 A O ATOM 1203 N VAL A 436 49.202 32.824 109.243 1.00 26.10 A N ATOM 1204 CA VAL A 436 48.123 32.238 108.461 1.00 27.17 A C ATOM 1205 CB VAL A 436 46.758 32.516 109.116 1.00 28.67 A C ATOM 1206 CG1 VAL A 436 45.651 31.841 108.322 1.00 28.01 A C ATOM 1207 CG2 VAL A 436 46.760 32.012 110.546 1.00 27.09 A C ATOM 1208 C VAL A 436 48.105 32.755 107.021 1.00 28.36 A C ATOM 1209 O VAL A 436 47.814 32.006 166.096 1.00 28.48 A O ATOM 1210 N ASN A 437 48.411 34.034 106.832 1.00 30.05 A N ATOM 1211 CA ASN A 437 48.449 34.604 105.488 1.00 32.08 A C ATOM 1212 CB ASN A 437 48.670 36.121 105.525 1.00 36.19 A C ATOM 1213 CG ASN A 437 47.464 36.875 106.018 1.00 40.19 A C ATOM 1214 OD1 ASN A 437 46.328 36.484 105.759 1.00 44.41 A O ATOM 1215 ND2 ASN A 437 47.701 37.978 106.719 1.00 44.69 A N ATOM 1216 C ASN A 437 49.589 33.983 104.701 1.00 30.92 A C ATOM 1217 O ASN A 437 49.406 33.559 103.565 1.00 31.67 A O ATOM 1218 N GLY A 438 50.768 33.946 105.315 1.00 27.54 A N ATOM 1219 CA GLY A 438 51.931 33.385 104.659 1.00 25.40 A C ATOM 1220 C GLY A 438 51.755 31.952 104.205 1.00 24.52 A C ATOM 1221 O GLY A 438 52.171 31.593 103.110 1.00 26.30 A O ATOM 1222 N ILE A 439 51.137 31.125 105.039 1.00 23.54 A N ATOM 1223 CA ILE A 439 50.943 29.732 104.681 1.00 23.31 A C ATOM 1224 CB ILE A 439 50.619 28.871 105.944 1.00 20.22 A C ATOM 1225 CG2 ILE A 439 49.210 29.136 106.450 1.00 18.09 A C ATOM 1226 CG1 ILE A 439 50.814 27.393 105.614 1.00 21.12 A C ATOM 1227 CD1 ILE A 439 52.238 27.048 105.201 1.00 14.56 A C ATOM 1228 C ILE A 439 49.867 29.547 103.593 1.00 24.64 A C ATOM 1229 O ILE A 439 50.017 28.712 102.705 1.00 25.35 A O ATOM 1230 N ARG A 440 48.793 30.324 103.649 1.00 23.43 A N ATOM 1231 CA ARG A 440 47.751 30.217 102.638 1.00 24.74 A C ATOM 1232 CB ARG A 440 46.481 30.932 103.091 1.00 25.89 A C ATOM 1233 CG ARG A 440 45.673 30.154 104.093 1.00 28.05 A C ATOM 1234 CD ARG A 440 44.453 30.927 104.518 1.00 33.06 A C ATOM 1235 NE ARG A 440 43.678 30.183 105.502 1.00 40.49 A N ATOM 1236 CZ ARG A 440 42.752 30.722 106.286 1.00 43.77 A C ATOM 1237 NH1 ARG A 440 42.485 32.020 106.205 1.00 45.47 A N ATOM 1238 NH2 ARG A 440 42.089 29.964 107.150 1.00 43.22 A N ATOM 1239 C ARG A 440 48.217 30.806 101.312 1.00 26.05 A C ATOM 1240 O ARO A 440 47.691 30.466 100.257 1.00 29.07 A O ATOM 1241 N HIS A 441 49.201 31.694 101.360 1.00 24.35 A N ATOM 1242 CA HIS A 441 49.707 32.290 100.139 1.00 24.72 A C ATOM 1243 CB HIS A 441 50.628 33.465 100.450 1.00 21.94 A C ATOM 1244 CG HiS A 441 50.942 34.308 99.255 1.00 21.49 A C ATOM 1245 CD2 HIS A 441 52.068 34.421 98.513 1.00 23.26 A C ATOM 1246 ND1 HIS A 441 50.018 35.152 98.679 1.00 23.21 A N ATOM 1247 CE1 HIS A 441 50.561 35.748 97.634 1.00 21.93 A C ATOM 1248 NE2 HIS A 441 51.804 35.322 97.512 1.00 24.09 A N ATOM 1249 C HIS A 441 50.463 31.238 99.332 1.00 26.24 A C ATOM 1250 O HIS A 441 50.531 31.313 98.104 1.00 26.96 A O ATOM 1251 N LEU A 442 51.028 30.260 100.032 1.00 27.09 A N ATOM 1252 CA LEU A 442 51.770 29.178 99.394 1.00 27.80 A C ATOM 1253 CB LEU A 442 52.861 28.648 100.329 1.00 28.49 A C ATOM 1254 CG LEU A 442 54.042 29.552 100.679 1.00 30.92 A C ATOM 1255 CD1 LEU A 442 54.898 28.875 101.737 1.00 31.60 A C ATOM 1256 CD2 LEU A 442 54.863 29.836 99.434 1.00 31.89 A C ATOM 1257 C LEU A 442 50.877 28.009 98.984 1.00 28.59 A C ATOM 1258 O LEU A 442 51.084 27.420 97.929 1.00 28.30 A O ATOM 1259 N TYR A 443 49.896 27.674 99.821 1.00 30.49 A N ATOM 1260 CA TYR A 443 48.993 26.553 99.548 1.00 31.37 A C ATOM 1261 CB TYR A 443 49.181 25.450 100.601 1.00 30.85 A C ATOM 1262 CG TYR A 443 50.611 24.990 100.753 1.00 28.19 A C ATOM 1263 CD1 TYR A 443 51.462 25.575 101.697 1.00 25.52 A C ATOM 1264 CE1 TYR A 443 52.805 25.190 101.793 1.00 23.19 A C ATOM 1265 CD2 TYR A 443 51.133 24.007 99.913 1.00 27.48 A C ATOM 1266 CE2 TYR A 443 52.469 23.617 100.000 1.00 26.82 A C ATOM 1267 CZ TYR A 443 53.298 24.213 100.937 1.00 24.13 A C ATOM 1268 OH TYR A 443 54.618 23.837 100.986 1.00 24.42 A O ATOM 1269 C TYR A 443 47.518 26.945 99.497 1.00 31.76 A C ATOM 1270 O TYR A 443 46.719 26.112 99.036 1.00 33.61 A O ATOM 1271 OT TYR A 443 47.163 28.054 99.935 1.00 33.91 A O ATOM 2560 ZN ZN A 1 63.267 29.950 112.382 1.00 18.93 Z ZN ATOM 2561 ZN ZN A 2 70.729 19.617 111.673 1.00 22.07 Z ZN ATOM 2565 CA CA A 3 71.413 25.140 121.665 1.00 25.39 C C ATOM 2566 CA CA A 4 63.107 15.179 103.757 1.00 28.86 C C ATOM 2567 CA CA A 5 67.687 17.476 126.440 1.00 49.10 C C ATOM 2568 CA CA A 6 57.389 24.336 131.008 1.00 56.13 C C ATOM 2573 CA CA A 7 41.603 20.860 107.667 1.00 99.94 C C ATOM 2515 C1 FRA A 1 62.295 30.885 117.488 1.00 16.45 M C ATOM 2516 C2 FRA A 1 63.038 29.608 117.942 1.00 19.42 M C ATOM 2517 C3 FRA A 1 61.951 28.564 118.122 1.00 18.32 M C ATOM 2518 C4 FRA A 1 64.019 29.134 116.841 1.00 18.44 M C ATOM 2519 C5 FRA A 1 65.268 30.026 116.452 1.00 20.30 M C ATOM 2520 C6 FRA A 1 66.093 29.344 115.298 1.00 21.58 M C ATOM 2521 N7 FRA A 1 65.323 29.140 114.074 1.00 19.54 M N ATOM 2522 O8 FRA A 1 65.083 30.177 113.358 1.00 20.40 M O ATOM 2523 C9 FRA A 1 64.851 27.958 113.673 1.00 20.49 M C ATOM 2524 O10 FRA A 1 64.213 27.793 112.689 1.00 19.70 M O ATOM 2525 C11 FRA A 1 66.274 30.187 117.629 1.00 22.72 M C ATOM 2526 N12 FRA A 1 66.450 31.428 118.131 1.00 21.65 M N ATOM 2527 C13 FRA A 1 67.389 31.754 119.271 1.00 23.60 M C ATOM 2528 C14 FRA A 1 68.279 33.067 118.969 1.00 24.52 M C ATOM 2529 C15 FRA A 1 69.263 33.407 120.153 1.00 23.38 M C ATOM 2530 C16 FRA A 1 67.424 34.373 118.736 1.00 23.95 M C ATOM 2531 C17 FRA A 1 69.119 32.883 117.677 1.00 21.36 M C ATOM 2532 C18 FRA A 1 66.491 31.847 120.586 1.00 23.15 M C ATOM 2533 O19 FRA A 1 65.406 32.468 120.589 1.00 24.19 M O ATOM 2534 N20 FRA A 1 67.003 31.196 121.667 1.00 21.19 M N ATOM 2535 C21 FRA A 1 66.350 31.137 122.996 1.00 25.36 M C ATOM 2536 O22 FRA A 1 66.882 29.180 118.067 1.00 22.29 M O ATOM 1273 CB ASP B 110 39.115 26.293 159.737 1.00 61.05 B C ATOM 1274 CG ASP B 110 39.042 27.399 160.776 1.00 62.86 B C ATOM 1275 OD1 ASP B 110 40.101 27.786 161.322 1.00 62.33 B O ATOM 1276 OD2 ASP B 110 37.917 27.876 161.046 1.00 63.37 B O ATOM 1277 C ASP B 110 40.865 24.867 160.849 1.00 56.49 B C ATOM 1278 O ASP B 110 41.355 25.782 161.519 1.00 56.57 B O ATOM 1279 N ASP B 110 38.439 24.617 161.434 1.00 58.69 B N ATOM 1280 CA ASP B 110 39.418 24.920 160.351 1.00 58.71 B C ATOM 1281 N LEU B 111 41.541 23.778 160.512 1.00 52.64 B N ATOM 1282 CA LEU B 111 42.921 23.579 160.910 1.00 48.28 B C ATOM 1283 CB LEU B 111 43.265 22.094 160.794 1.00 48.88 B C ATOM 1284 CG LEU B 111 44.509 21.605 161.528 1.00 50.33 B C ATOM 1285 CD1 LEU B 111 44.535 22.156 162.948 1.00 50.73 B C ATOM 1286 CD2 LEU B 111 44.500 20.088 161.540 1.00 51.89 B C ATOM 1287 C LEU B 111 43.846 24.419 160.029 1.00 43.58 B C ATOM 1288 O LEU B 111 43.584 24.607 158.838 1.00 42.86 B O ATOM 1289 N LYS B 112 44.917 24.942 160.615 1.00 37.78 B N ATOM 1290 CA LYS B 112 45.858 25.745 159.846 1.00 34.84 B C ATOM 1291 CB LYS B 112 45.341 27.176 159.702 1.00 35.26 B C ATOM 1292 CG LYS B 112 45.439 28.007 160.972 1.00 39.03 B C ATOM 1293 CD LYS B 112 45.160 29.466 160.674 1.00 38.56 B C ATOM 1294 CE LYS B 112 45.529 30.353 161.845 1.00 41.04 B C ATOM 1295 NZ LYS B 112 45.396 31.790 161.475 1.00 41.35 B N ATOM 1296 C LYS B 112 47.233 25.767 160.498 1.00 32.44 B C ATOM 1297 O LYS B 112 47.395 25.317 161.628 1.00 31.94 B O ATOM 1298 N TRP B 113 48.225 26.284 159.779 1.00 30.35 B N ATOM 1299 CA TRP B 113 49.571 26.359 160.320 1.00 30.31 B C ATOM 1300 CB TRP B 113 50.613 26.516 159.204 1.00 27.93 B C ATOM 1301 CG TRP B 113 50.690 25.351 158.258 1.00 27.86 B C ATOM 1302 CD2 TRP B 113 51.204 24.040 158.541 1.00 26.96 B C ATOM 1303 CE2 TRP B 113 51.058 23.271 157.363 1.00 27.29 B C ATOM 1304 CE3 TRP B 113 51.773 23.441 159.674 1.00 23.04 B C ATOM 1305 CD1 TRP B 113 50.266 25.321 156.958 1.00 26.75 B C ATOM 1306 NE1 TRP B 113 50.483 24.078 156.415 1.00 23.61 B N ATOM 1307 CZ2 TRP B 113 51.460 21.930 157.287 1.00 24.46 B C ATOM 1308 CZ3 TRP B 113 52.171 22.108 159.597 1.00 23.32 B C ATOM 1309 CH2 TRP B 113 52.012 21.369 158.410 1.00 23.78 B C ATOM 1310 C TRP B 113 49.645 27.558 161.252 1.00 31.82 B C ATOM 1311 O TRP B 113 49.024 28.589 160.996 1.00 32.51 B O ATOM 1312 N HIS B 114 50.400 27.419 162.335 1.00 31.20 B N ATOM 1313 CA HIS B 114 50.549 28.507 163.285 1.00 31.82 B C ATOM 1314 CB HIS B 114 50.577 27.963 164.711 1.00 31.55 B C ATOM 1315 CG HIS B 114 49.237 27.513 165.193 1.00 32.54 B C ATOM 1316 CD2 HIS B 114 47.999 27.711 164.681 1.00 32.52 B C ATOM 1317 ND1 HIS B 114 49.064 26.767 166.337 1.00 33.18 B N ATOM 1318 CE1 HIS B 114 47.777 26.523 166.510 1.00 32.64 B C ATOM 1319 NE2 HIS B 114 47.110 27.085 165.518 1.00 34.29 B N ATOM 1320 C HIS B 114 51.774 29.357 163.006 1.00 30.66 B C ATOM 1321 O HIS B 114 51.997 30.358 163.679 1.00 34.99 B O ATOM 1322 N HIS B 115 52.572 28.950 162.022 1.00 28.55 B N ATOM 1323 CA HIS B 115 53.245 29.722 161.617 1.00 25.56 B C ATOM 1324 CB HIS B 115 55.044 28.934 161.824 1.00 25.76 B C ATOM 1325 CG HIS B 115 55.057 27.591 161.164 1.00 25.72 B C ATOM 1326 CD2 HIS B 115 55.839 27.090 160.180 1.00 24.52 B C ATOM 1327 ND1 HIS B 115 54.198 26.576 161.526 1.00 24.79 B N ATOM 1328 CE1 HIS B 115 54.453 25.506 160.796 1.00 22.93 B C ATOM 1329 NE2 HIS B 115 55.445 25.791 159.971 1.00 23.07 B N ATOM 1330 C HIS B 115 53.553 30.058 160.144 1.00 25.78 B C ATOM 1331 O HIS B 115 52.775 29.406 159.456 1.00 26.11 B O ATOM 1332 N HIS B 116 54.261 31.072 159.666 1.00 25.82 B N ATOM 1333 CA HIS B 116 54.133 31.514 158.286 1.00 25.15 B C ATOM 1334 CB HIS B 116 53.911 33.030 158.253 1.00 25.12 B C ATOM 1335 CG HIS H 116 52.559 33.446 158.740 1.00 26.86 B C ATOM 1336 CD2 HIS B 116 51.495 32.712 159.144 1.00 25.46 B C ATOM 1337 ND1 HIS B 116 52.177 34.766 158.840 1.00 26.98 B N ATOM 1338 GE1 HIS B 116 50.934 34.826 159.285 1.00 29.50 B C ATOM 1339 NE2 HIS B 116 50.498 33.594 159.477 1.00 28.22 B N ATOM 1340 C HIS B 116 55.290 31.152 157.372 1.00 24.84 B C ATOM 1341 O HIS B 116 55.163 31.228 156.155 1.00 24.51 B O ATOM 1342 N ASN B 117 56.421 30.779 157.955 1.00 23.92 B N ATOM 1343 CA ASN B 117 57.581 30.395 157.166 1.00 23.42 B C ATOM 1344 CB ASN B 117 58.868 30.914 157.824 1.00 24.61 B C ATOM 1345 CG ASN B 117 59.019 30.486 159.285 1.00 27.08 B C ATOM 1346 OD1 ASN B 117 58.047 30.395 160.041 1.00 28.75 B O ATOM 1347 ND2 ASN B 117 60.259 30.244 159.689 1.00 24.54 B N ATOM 1348 C ASN B 117 57.568 28.878 157.046 1.00 23.79 B C ATOM 1349 O ASN B 117 58.249 28.160 157.779 1.00 22.99 B O ATOM 1350 N ILE B 118 56.760 28.401 156.107 1.00 23.12 B N ATOM 1351 CA ILE B 118 56.585 26.979 155.876 1.00 24.05 B C ATOM 1352 CB ILE B 118 55.245 26.734 155.156 1.00 25.87 B C ATOM 1353 CG2 ILE B 118 55.066 25.256 154.855 1.00 25.54 B C ATOM 1354 CG1 ILE B 118 54.104 27.259 156.039 1.00 26.83 B C ATOM 1355 CD1 ILE B 118 52.721 27.053 155.465 1.00 31.75 B C ATOM 1356 C ILE B 118 57.722 26.340 155.097 1.00 23.08 B C ATOM 1357 O ILE B 118 58.319 26.962 154.223 1.00 25.00 B O ATOM 1358 N THR B 119 58.029 25.094 155.429 1.00 21.12 B N ATOM 1359 CA THR B 119 59.096 24.382 154.744 1.00 19.30 B C ATOM 1360 CB THR B 119 60.203 23.938 155.721 1.00 18.41 B C ATOM 1361 OG1 THR B 119 59.640 23.097 156.732 1.00 18.81 B O ATOM 1362 CG2 THR B 119 60.861 25.147 156.359 1.00 14.91 B C ATOM 1363 C THR B 119 58.564 23.156 154.026 1.00 18.87 B C ATOM 1364 O THR B 119 57.539 22.586 154.415 1.00 17.08 B O ATOM 1365 N TYR B 120 59.260 22.756 152.966 1.00 18.82 B N ATOM 1366 CA TYR B 120 58.848 21.584 152.207 1.00 17.71 B C ATOM 1367 CB TYR B 120 57.966 21.973 151.004 1.00 14.12 B C ATOM 1368 CG TYR B 120 58.671 22.725 149.891 1.00 14.85 B C ATOM 1369 CD1 TYR B 120 58.811 24.113 149.936 1.00 15.43 B C ATOM 1370 CE1 TYR B 120 59.392 24.817 148.882 1.00 12.87 B C ATOM 1371 CD2 TYR B 120 59.144 22.052 148.761 1.00 15.15 B C ATOM 1372 CE2 TYR B 120 59.725 22.746 147.702 1.00 15.56 B C ATOM 1373 CZ TYR B 120 59.842 24.126 147.766 1.00 17.67 B C ATOM 1374 OH TYR B 120 60.378 24.816 146.702 1.00 20.47 B O ATOM 1375 C TYR B 120 60.048 20.798 151.726 1.00 14.81 B C ATOM 1376 O TYR B 120 61.116 21.353 151.497 1.00 14.65 B O ATOM 1377 N TRP B 121 59.840 19.499 151.567 1.00 12.91 B N ATOM 1378 CA TRP B 121 60.867 18.587 151.121 1.00 14.27 B C ATOM 1379 CB TRP B 121 61.271 17.677 152.295 1.00 16.23 B C ATOM 1380 CO TRP B 121 62.237 16.559 151.970 1.00 16.27 B C ATOM 1381 CD2 TRP B 121 62.292 15.266 152.595 1.00 17.47 B C ATOM 1382 CE2 TRP B 121 63.424 14.600 152.078 1.00 17.45 B C ATOM 1383 CE3 TRP B 121 61.496 14.610 153.S48 1.00 17.63 B C ATOM 1384 CD1 TRP B 121 63.303 16.613 151.117 1.00 17.04 B C ATOM 1385 NE1 TRP B 121 64.021 15.442 151.179 1.00 16.74 B N ATOM 1386 CZ2 TRP B 121 63.783 13.307 152.484 1.00 18.60 B C ATOM 1387 CZ3 TRP B 121 61.853 13.327 153.952 1.00 18.18 B C ATOM 1388 CH2 TRP B 121 62.988 12.691 153.420 1.00 18.22 B C ATOM 1389 C TRP B 121 60.355 17.741 149.955 1.00 15.49 B C ATOM 1390 O TRP B 121 59.312 17.093 150.061 1.00 13.62 B O ATOM 1391 N ILE B 122 61.080 17.770 148.841 1.00 12.10 B N ATOM 1392 CA ILE B 122 60.729 16.956 147.696 1.00 13.59 B C ATOM 1393 CB ILE B 122 61.167 17.608 146.381 1.00 14.78 B C ATOM 1394 CG2 ILE B 122 60.773 16.715 145.214 1.00 10.29 B C ATOM 1395 CO1 ILE B 122 60.520 18.991 146.254 1.00 13.64 B C ATOM 1396 CD1 ILE B 122 61.024 19.811 145.080 1.00 12.29 B C ATOM 1397 C ILE B 122 61.514 15.672 147.918 1.00 13.64 B C ATOM 1398 O ILE B 122 62.694 15.588 147.592 1.00 14.54 B O ATOM 1399 N GLN B 123 60.855 14.679 148.496 1.00 13.68 B N ATOM 1400 CA GLN B 123 61.496 13.413 148.802 1.00 15.77 B C ATOM 1401 CB GLN B 123 60.564 12.573 149.662 1.00 14.28 B C ATOM 1402 CG GLN B 123 61.092 11.200 149.957 1.00 19.68 B C ATOM 1403 CD GLN B 123 60.133 10.402 150.794 1.00 22.52 B C ATOM 1404 OE1 GLN B 123 59.933 9.211 150.560 1.00 28.95 B O ATOM 1405 NE2 GLN B 123 59.534 11.048 151.782 1.00 19.79 B N ATOM 1406 C GLN B 123 61.971 12.587 147.604 1.00 18.55 B C ATOM 1407 O GLN B 123 63.086 12.069 147.611 1.00 18.76 B O ATOM 1408 N ASN B 124 61.118 12.428 146.596 1.00 19.57 B N ATOM 1409 CA ASN B 124 61.492 11.664 145.412 1.00 17.91 B C ATOM 1410 CB ASN B 124 61.111 10.184 145.549 1.00 17.29 B C ATOM 1411 CG ASN B 124 59.628 9.965 145.734 1.00 18.23 B C ATOM 1412 OD1 ASN B 124 58.830 10.882 145.602 1.00 20.83 B O ATOM 1413 ND2 ASN B 124 59.254 8.735 146.035 1.00 18.51 B N ATOM 1414 C ASN B 124 60.868 12.265 144.165 1.00 19.24 B C ATOM 1415 O ASN B 124 60.138 13.261 144.239 1.00 19.36 B O ATOM 1416 N TYR B 125 61.164 11.666 143.016 1.00 18.73 B N ATOM 1417 CA TYR B 125 60.670 12.187 141.749 1.00 14.58 B C ATOM 1418 CB TYR B 125 61.844 12.731 140.921 1.00 15.39 B C ATOM 1419 CG TYR B 125 62.538 13.932 141.536 1.00 13.70 B C ATOM 1420 CD1 TYR B 125 63.526 13.777 142.510 1.00 12.60 B C ATOM 1421 CE1 TYR B 125 64.113 14.889 143.124 1.00 11.44 B C ATOM 1422 CD2 TYR B 125 62.156 15.229 141.187 1.00 15.12 B C ATOM 1423 CE2 TYR B 125 62.731 16.341 141.793 1.00 11.78 B C ATOM 1424 CZ TYR B 125 63.706 16.164 142.760 1.00 13.63 B C ATOM 1425 OH TYR B 125 64.257 17.270 143.365 1.00 11.62 B O ATOM 1426 C TYR B 125 59.890 11.203 140.899 1.00 14.07 B C ATOM 1427 O TYR B 125 59.880 10.005 141.158 1.00 12.64 B O ATOM 1428 N SER B 126 59.230 11.737 139.877 1.00 15.52 B N ATOM 1429 CA SER B 126 58.461 10.929 138.936 1.00 17.11 B C ATOM 1430 CB SER B 126 57.246 11.705 138.419 1.00 17.11 B C ATOM 1431 OG SER B 126 56.716 11.100 137.252 1.00 14.91 B O ATOM 1432 C SER B 126 59.374 10.596 137.766 1.00 20.19 B C ATOM 1433 O SER B 126 60.298 11.345 137.452 1.00 19.00 B O ATOM 1434 N GLU B 127 59.109 9.480 137.108 1.00 23.95 B N ATOM 1435 CA GLU B 127 59.937 9.079 135.982 1.00 27.98 B C ATOM 1436 CB GLU B 127 59.795 7.575 135.743 1.00 33.47 B C ATOM 1437 CG GLU B 127 59.913 6.740 137.004 1.00 40.62 B C ATOM 1438 CD GLU B 127 60.077 5.255 136.718 1.00 45.97 B C ATOM 1439 OE1 GLU B 127 61.082 4.880 136.068 1.00 47.09 B O ATOM 1440 OE2 GLU B 127 59.204 4.466 137.148 1.00 47.02 B O ATOM 1441 C GLU B 127 59.585 9.825 134.700 1.00 26.19 B C ATOM 1442 O GLU B 127 60.331 9.763 133.732 1.00 27.48 B O ATOM 1443 N ASP B 128 58.464 10.543 134.702 1.00 23.99 B N ATOM 1444 CA ASP B 128 58.008 11.256 133.511 1.00 21.74 B C ATOM 1445 CB ASP B 128 56.496 11.480 133.557 1.00 22.01 B C ATOM 1446 CG ASP B 128 55.717 10.228 133.884 1.00 18.40 B C ATOM 1447 OD1 ASP B 128 56.138 9.119 133.514 1.00 21.04 B O ATOM 1448 OD2 ASP B 128 54.652 10.371 134.504 1.00 17.97 B O ATOM 1449 C ASP B 128 58.637 12.606 133.194 1.00 22.03 B C ATOM 1450 O ASP B 128 58.578 13.052 132.0Sf 1.00 21.61 B O ATOM 1451 N LEU B 129 59.207 13.273 134.189 1.00 19.22 B N ATOM 1452 CA LEU B 129 59.797 14.582 133.953 1.00 17.22 B C ATOM 1453 CB LEU B 129 58.887 15.664 134.528 1.00 16.52 B C ATOM 1454 CG LEU B 129 57.497 15.796 133.901 1.00 20.26 B C ATOM 1455 CD1 LEU B 129 56.642 16.745 134.732 1.00 18.39 B C ATOM 1456 CD2 LEU B 129 57.629 16.303 132.471 1.00 19.31 B C ATOM 1457 C LEU B 129 61.179 14.713 134.566 1.00 17.81 B C ATOM 1458 O LEU B 129 61.515 14.000 135.511 1.00 20.83 B O ATOM 1459 N PRO B 130 62.014 15.617 134.021 1.00 17.25 B N ATOM 1460 CD PRO B 130 61.811 16.408 132.796 1.00 15.36 B C ATOM 1461 CA PRO B 130 63.371 15.820 134.557 1.00 17.25 B C ATOM 1462 CB PRO B 130 64.002 16.790 133.554 1.00 14.93 B C ATOM 1463 CG PRO B 130 63.214 16.559 132.292 1.00 15.96 B C ATOM 1464 C PRO B 130 63.250 16.450 135.954 1.00 15.64 B C ATOM 1465 O PRO B 130 62.245 17.096 136.250 1.00 15.44 B O ATOM 1466 N ARG B 131 64.259 16.265 136.805 1.00 16.42 B N ATOM 1467 CA ARG B 131 64.237 16.840 138.159 1.00 16.86 B C ATOM 1468 CB ARG B 131 65.551 16.591 138.906 1.00 18.20 B C ATOM 1469 CG ARG B 131 65.708 15.207 139.469 1.00 22.57 B C ATOM 1470 CD ARG B 131 66.845 15.143 140.470 1.00 21.69 B C ATOM 1471 NE ARG B 131 67.022 13.771 140.932 1.00 26.97 B N ATOM 1472 CZ ARG B 131 67.541 13.427 142.107 1.00 28.81 B C ATOM 1473 NH1 ARG B 131 67.945 14.360 142.966 1.00 24.33 B N ATOM 1474 NH2 ARG B 131 67.641 12.143 142.424 1.00 28.78 B N ATOM 1475 C ARG B 131 64.022 18.338 138.138 1.00 16.07 B C ATOM 1476 O ARG B 131 63.219 18.869 138.899 1.00 15.45 B O ATOM 1477 N ALA B 132 64.764 19.013 137.268 1.00 14.39 B N ATOM 1478 CA ALA B 132 64.685 20.461 137.163 1.00 16.40 B C ATOM 1479 CB ALA B 132 65.677 20.959 136.106 1.00 17.38 B C ATOM 1480 C ALA B 132 63.278 20.946 136.837 1.00 16.67 B C ATOM 1481 O ALA B 132 62.844 21.984 137.326 1.00 18.93 B O ATOM 1482 N VAL B 133 62.566 20.192 136.008 1.00 15.47 B N ATOM 1483 CA VAL B 133 61.213 20.562 135.626 1.00 13.45 B C ATOM 1484 CB VAL B 133 60.721 19.694 134.433 1.00 14.12 B C ATOM 1485 CG1 VAL B 133 59.229 19.926 134.177 1.00 9.73 B C ATOM 1486 CO2 VAL B 133 61.530 20.037 133.190 1.00 12.36 B C ATOM 1487 C VAL B 133 60.259 20.394 136.803 1.00 14.22 B C ATOM 1488 O VAL B 133 59.362 21.211 137.016 1.00 13.15 B O ATOM 1489 N ILE B 134 60.460 19.323 137.563 1.00 15.06 B N ATOM 1490 CA ILE B 134 59.617 19.029 138.709 1.00 13.17 B C ATOM 1491 GB ILE B 134 59.855 17.580 139.200 1.00 14.87 B C ATOM 1492 CG2 ILE B 134 59.229 17.371 140.571 1.00 14.89 B C ATOM 1493 CG1 ILE B 134 59.287 16.597 138.166 1.00 11.36 B C ATOM 1494 CD1 ILE B 134 59.476 15.131 138.521 1.00 11.57 B C ATOM 1495 C ILE B 134 59.862 20.025 139.830 1.00 15.99 B C ATOM 1496 O ILE B 134 58.908 20.543 140.404 1.00 16.24 B O ATOM 1497 N ASP B 135 61.132 20.308 140.134 1.00 15.66 B N ATOM 1498 CA ASP B 135 61.447 21.279 141.184 1.00 15.15 B C ATOM 1499 CB ASP B 135 62.959 21.544 141.288 1.00 12.56 B C ATOM 1SOO CG ASP B 135 63.746 20.351 141.803 1.00 10.35 B C ATOM 1501 OD1 ASP B 135 63.156 19.399 142.353 1.00 11.63 B O ATOM 1502 OD2 ASP B 135 64.983 20.371 141.664 1.00 17.25 B O ATOM 1503 C ASP B 135 60.752 22.603 140.871 1.00 15.48 B C ATOM 1504 O ASP B 135 60.095 23.187 141.732 1.00 20.45 B O ATOM 1505 N ASP B 136 60.902 23.069 139.635 1.00 14.76 B N ATOM 1506 CA ASP B 136 60.313 24.328 139.189 1.00 13.88 B C ATOM 1507 CB ASP B 136 60.768 24.621 137.762 1.00 16.77 B C ATOM 1508 CG ASP B 136 60.207 25.919 137.221 1.00 19.24 B C ATOM 1509 OD1 ASP B 136 60.611 26.985 137.721 1.00 20.16 B O ATOM 1510 OD2 ASP B 136 59.362 25.870 136.297 1.00 18.28 B O ATOM 1511 C ASP B 136 58.785 24.354 139.267 1.00 13.68 B C ATOM 1512 O ASP B 136 58.200 25.343 139.697 1.00 18.58 B O ATOM 1513 N ALA B 137 58.135 23.276 138.850 1.00 12.86 B N ATOM 1514 CA ALA B 137 56.679 23.204 138.907 1.00 10.91 B C ATOM 1515 CB ALA B 137 56.196 21.882 138.315 1.00 9.57 B C ATOM 1516 C ALA B 137 56.174 23.343 140.347 1.00 13.69 B C ATOM 1517 O ALA B 137 55.184 24.034 140.601 1.00 14.16 B O ATOM 1518 N PHE B 138 56.831 22.668 141.289 1.00 15.83 B N ATOM 1519 CA PHE B 138 56.425 22.758 142.694 1.00 16.29 B C ATOM 1520 CB PHE B 138 57.182 21.737 143.559 1.00 13.24 B C ATOM 1521 CG PHE B 138 56.731 20.304 143.363 1.00 12.26 B C ATOM 1522 CD1 PHE B 138 55.409 20.007 143.025 1.00 13.72 B C ATOM 1523 CD2 PHE B 138 57.628 19.251 143.516 1.00 9.81 B C ATOM 1524 CE1 PHE B 138 54.995 18.679 142.841 1.00 13.46 B C ATOM 1525 CE2 PHE B 138 57.224 17.927 143.337 1.00 7.35 B C ATOM 1526 CZ PHE B 138 55.907 17.641 142.998 1.00 11.80 B C ATOM 1527 C PHE B 138 56.670 24.172 143.226 1.00 16.78 B C ATOM 1528 O PHE B 138 55.871 24.709 143.990 1.00 19.28 B O ATOM 1529 N ALA B 139 57.772 24.783 142.807 1.00 17.38 B N ATOM 1530 CA ALA B 139 58.093 26.136 143.246 1.00 17.57 B C ATOM 1531 CB ALA B 139 59.490 26.521 142.770 1.00 14.41 B C ATOM 1532 C ALA B 139 57.061 27.149 142.738 1.00 18.95 B C ATOM 1533 O ALA B 139 56.664 28.060 143.467 1.00 19.80 B O ATOM 1534 N ARG B 140 56.628 26.993 141.490 1.00 19.15 B N ATOM 1535 CA ARG B 140 55.642 27.906 140.917 1.00 17.98 B C ATOM 1536 CB ARG B 140 55.596 27.761 139.388 1.00 16.03 B C ATOM 1537 CG ARG B 140 56.888 28.201 138.707 1.00 16.18 B C ATOM 1538 CD ARG B 140 56.812 28.138 137.181 1.00 18.32 B C ATOM 1539 NE ARG B 140 56.746 26.768 136.685 1.00 14.27 B N ATOM 1540 CZ ARG B 140 55.666 26.213 136.150 1.00 14.50 B C ATOM 1541 NE1 ARG B 140 54.548 26.912 136.030 1.00 12.39 B N ATOM 1542 NH2 ARG B 140 55.701 24.946 135.753 1.00 14.50 B N ATQM 1543 C ARG B 140 54.274 27.638 141.531 1.00 18.29 B C ATOM 1544 O ARG B 140 53.451 28.544 141.661 1.00 22.02 B O ATOM 1545 N ALA B 141 54.036 26.392 141.927 1.00 17.80 B N ATOM 1546 CA ALA B 141 52.768 26.030 142.552 1.00 17.21 B C ATOM 1547 CB ALA B 141 52.656 24.520 142.660 1.00 17.90 B C ATOM 1548 C ALA B 141 52.660 26.677 143.941 1.00 19.87 B C ATOM 1549 O ALA B 141 51.572 27.056 144.369 1.00 19.56 B O ATOM 1550 N PHE B 142 53.787 26.795 144.645 1.00 20.99 B N ATOM 1551 CA PHE B 142 53.798 27.427 145.970 1.00 21.67 B C ATOM 1552 CB PHE B 142 55.072 27.069 146.759 1.00 18.85 B C ATOM 1553 CG PHE B 142 55.008 25.734 147.446 1.00 16.57 B C ATOM 1554 CD1 PHE B 142 53.976 25.449 148.333 1.00 14.21 B C ATOM 1555 CD2 PHE B 142 55.974 24.764 147.204 1.00 14.86 B C ATOM 1556 CE1 PHE B 142 53.904 24.220 148.972 1.00 18.27 B C ATOM 1557 CE2 PHE B 142 55.917 23.527 147.836 1.00 19.57 B C ATOM 1558 CZ PHE B 142 54.879 23.251 148.724 1.00 20.55 B C ATOM 1559 C PHE B 142 53.719 28.942 145.832 1.00 21.95 B C ATOM 1560 O PHE B 142 53.101 29.613 146.652 1.00 25.86 B O ATOM 1561 N ALA B 143 54.356 29.481 144.802 1.00 20.87 B N ATOM 1562 CA ALA B 143 54.344 30.921 144.576 1.00 21.45 B C ATOM 1563 CB ALA B 143 55.222 31.268 143.390 1.00 17.43 B C ATOM 1564 C ALA B 143 52.930 31.466 144.360 1.00 23.06 B C ATOM 1565 O ALA B 143 52.661 32.629 144.658 1.00 25.48 B O ATOM 1566 N LEU B 144 52.029 30.636 143.841 1.00 24.74 B N ATOM 1567 CA LEU B 144 50.652 31.075 143.615 1.00 26.04 D C ATOM 1568 CB LEU B 144 49.797 29.958 143.010 1.00 24.21 B C ATOM 1569 CG LEU B 144 49.951 29.560 141.539 1.00 27.50 B C ATOM 1570 CD1 LEU B 144 48.945 28.468 141.230 1.00 25.16 B C ATOM 1571 CD2 LEU B 144 49.718 30.754 140.630 1.00 23.79 B C ATOM 1572 C LEU B 144 50.020 31.481 144.934 1.00 28.47 B C ATOM 1573 O LEU B 144 49.343 32.500 145.030 1.00 30.66 B O ATOM 1574 N TRP B 145 50.245 30.664 145.951 1.00 28.49 B N ATOM 1575 CA TRP B 145 49.680 30.913 147.265 1.00 29.54 B C ATOM 1576 CB TRP B 145 49.652 29.609 148.053 1.00 26.39 B C ATOM 1577 CG TRP B 145 48.796 28.553 147.417 1.00 24.57 B C ATOM 1578 CD2 TRP B 145 47.366 28.550 147.330 1.00 25.64 B C ATOM 1579 CE2 TRP B 145 46.986 27.320 146.747 1.00 24.80 B C ATOM 1580 CE3 TRP B 145 46.366 29.464 147.695 1.00 25.42 B C ATOM 1581 CD1 TRP B 145 49.214 27.369 146.885 1.00 22.40 B C ATOM 1582 NE1 TRP B 145 48.133 26.619 146.483 1.00 22.24 B N ATOM 1583 CZ2 TRP B 145 45.644 26.977 146.522 1.00 27.07 B C ATOM 1584 CZ3 TRP B 145 45.029 29.122 147.471 1.00 26.11 B C ATOM 1585 CH2 TRP B 145 44.684 27.889 146.892 1.00 24.97 B C ATOM 1586 C TRP B 145 50.397 31.995 148.064 1.00 28.97 B C ATOM 1587 O TRY B 145 49.752 32.844 148.674 1.00 29.64 B O ATOM 1588 N SER B 146 51.724 31.979 148.063 1.00 30.94 B N ATOM 1589 CA SER B 146 52.474 32.986 148.808 1.00 33.11 B C ATOM 1590 CB SER B 146 53.967 32.675 148.776 1.00 31.16 B C ATOM 1591 OG SER B 146 54.465 32.773 147.457 1.00 34.33 B O ATOM 1592 C SER B 146 52.241 34.372 148.221 1.00 35.39 B C ATOM 1593 O SER B 146 52.600 35.381 148.827 1.00 38.15 B O ATOM 1594 N ALA B 147 51.641 34.418 147.039 1.00 35.46 B N ATOM 1595 CA ALA B 147 51.379 35.683 146.374 1.00 35.64 B C ATOM 1596 CB ALA B 147 51.187 35.457 144.883 1.00 35.78 B C ATOM 1597 C ALA B 147 50.160 36.380 146.949 1.00 36.30 B C ATOM 1598 O ALA B 147 50.054 37.600 146.875 1.00 35.93 B O ATOM 1599 N VAL B 148 49.238 35.611 147.519 1.00 36.26 B N ATOM 1600 CA VAL B 148 48.031 36.196 148.089 1.00 37.29 B C ATOM 1601 GB VAL B 148 46.761 35.601 147.435 1.00 37.45 B C ATOM 1602 CG1 VAL B 148 46.728 35.952 145.959 1.00 39.35 B C ATOM 1603 CG2 VAL B 148 46.735 34.099 147.614 1.00 37.42 B C ATOM 1604 C VAL B 148 47.926 36.035 149.606 1.00 37.54 B C ATOM 1605 O VAL B 148 46.838 36.144 150.173 1.00 38.76 B O ATOM 1606 N THR B 149 49.057 35.774 150.257 1.00 36.72 B N ATOM 1607 CA THR B 149 49.098 35.611 151.711 1.00 34.50 B C ATOM 1608 GB THR B 149 48.815 34.159 152.139 1.00 32.69 B C ATOM 1609 OG1 THR B 149 49.872 33.313 151.672 1.00 34.10 B O ATOM 1610 CG2 THR B 149 47.492 33.677 151.587 1.00 33.09 B C ATOM 1611 C THR B 149 50.484 35.975 152.241 1.00 34.43 B C ATOM 1612 O THR B 149 51.424 36.166 151.466 1.00 33.86 B O ATOM 1613 N PRO B 150 50.624 36.084 153.576 1.00 35.88 B N ATOM 1614 CD PRO B 150 49.542 36.096 154.582 1.00 36.97 B C ATOM 1615 CA PRO B 150 51.909 36.423 154.199 1.00 35.29 B C ATOM 1616 GB PRO B 150 51.491 36.993 155.548 1.00 33.79 B C ATOM 1617 CG PRO B 150 50.313 36.136 155.894 1.00 36.98 B C ATOM 1618 C PRO B 150 52.810 35.190 154.341 1.00 33.55 B C ATOM 1619 O PRO B 150 53.889 35.259 154.928 1.00 33.85 B O ATOM 1620 N LEU B 151 52.357 34.064 153.796 1.00 32.24 B N ATOM 1621 CA LEU B 151 53.111 32.813 153.850 1.00 29.72 B C ATOM 1622 CB LEU B 151 52.210 31.634 153.485 1.00 28.34 B C ATOM 1623 CG LEU B 151 50.920 31.386 154.263 1.00 29.72 B C ATOM 1624 CD1 LEU B 151 50.115 30.308 153.547 1.00 25.73 B C ATOM 1625 CD2 LEU B 151 51.241 30.971 155.697 1.00 27.68 B C ATOM 1626 C LEU B 151 54.301 32.796 152.897 1.00 28.80 B C ATOM 1627 O LEU B 151 54.253 33.384 151.817 1.00 29.79 B O ATOM 1628 N THR B 152 55.370 32.123 153.307 1.00 26.47 B N ATOM 1629 CA THR B 152 56.550 31.968 152.468 1.00 26.48 B C ATOM 1630 GB THR B 152 57.786 32.697 153.018 1.00 25.05 B C ATOM 1631 OG1 THR B 152 58.199 32.092 154.250 1.00 26.56 B O ATOM 1632 CG2 THR B 152 57.478 34.161 153.235 1.00 26.91 B C ATOM 1633 C THR B 152 56.822 30.469 152.444 1.00 27.63 B C ATOM 1634 O THR B 152 56.361 29.731 153.321 1.00 28.65 B O ATOM 1635 N PHE B 153 57.561 30.020 151.438 1.00 26.34 B N ATOM 1636 CA PHE B 153 57.858 28.603 151.289 1.00 24.22 B C ATOM 1637 GB PHE B 153 57.010 28.041 150.147 1.00 21.10 B C ATOM 1638 CG PHE B 153 55.531 28.101 150.419 1.00 21.18 B C ATOM 1639 CD1 PHE B 153 54.916 27.141 151.229 1.00 19.72 B C ATOM 1640 CD2 PHE B 153 54.761 29.150 149.924 1.00 18.40 B C ATOM 1641 CE1 PHE B 153 53.560 27.231 151.541 1.00 18.13 B C ATOM 1642 CE2 PHE B 153 53.404 29.249 150.231 1.00 15.81 B C ATOM 1643 CZ PHE B 153 52.803 28.291 151.040 1.00 17.61 B C ATOM 1644 C PHE B 153 59.338 28.362 151.045 1.00 23.36 B C ATOM 1645 O PHE B 153 59.910 28.853 150.079 1.00 25.84 B O ATOM 1646 N THR B 154 59.951 27.596 151.938 1.00 24.03 B N ATOM 1647 CA THR B 154 61.375 27.302 151.858 1.00 22.52 B C ATOM 1648 CB THR B 154 62.075 27.739 153.149 1.00 21.34 B C ATOM 1649 OG1 THR B 154 61.867 29.138 153.328 1.00 25.73 B O ATOM 1650 CG2 THR B 154 63.567 27.461 153.091 1.00 20.97 B C ATOM 1651 C THR B 154 61.629 25.824 151.638 1.00 21.11 B C ATOM 1652 O THR B 154 61.050 24.977 152.317 1.00 21.31 B O ATOM 1653 N ARG B 155 62.502 25.521 150.688 1.00 21.15 B N ATOM 1654 CA ARG B 155 62.831 24.138 150.385 1.00 21.88 B C ATOM 1655 CB ARG B 155 63.248 23.996 148.919 1.00 23.11 B C ATOM 1656 CC ARG B 155 63.532 22.559 148.524 1.00 20.37 B C ATOM 1657 CD ARG B 155 64.052 22.459 147.121 1.00 21.66 B C ATOM 1658 NE ARG B 155 64.381 21.083 146.772 1.00 18.52 B N ATOM 1659 CZ ARG B 155 64.905 20.721 145.610 1.00 17.45 B C ATOM 1660 NH1 ARC B 155 65.158 21.637 144.689 1.00 16.66 B N ATOM 1661 NH2 ARG B 155 65.174 19.447 145.372 1.00 15.63 B N ATOM 1662 C ARG B 155 63.963 23.657 151.284 1.00 22.35 B C ATOM 1663 O ARC B 155 64.973 24.341 151.435 1.00 23.6S B O ATOM 1664 N VAL B 156 63.784 22.486 151.888 1.00 21.22 B N ATOM 1665 CA VAL B 156 64.795 21.904 152.760 1.00 21.38 B C ATOM 1666 CB VAL B 156 64.384 22.006 154.252 1.00 21.61 B C ATOM 1667 CO1 VAL B 156 64.096 23.462 154.600 1.00 19.88 B C ATOM 1668 CO2 VAL B 156 63.158 21.135 154.537 1.00 20.58 B C ATOM 1669 C VAL B 156 64.951 20.447 152.345 1.00 23.15 B C ATOM 1670 O VAL B 156 64.240 19.988 151.456 1.00 23.36 B O ATOM 1671 N TYR B 157 65.864 19.717 152.982 1.00 24.51 B N ATOM 1672 CA TYR B 157 66.100 18.321 152.613 1.00 25.70 B C ATOM 1673 CB TYR B 157 67.475 18.190 151.956 1.00 23.43 B C ATOM 1674 CG TYR B 157 67.634 19.050 150.728 1.00 23.94 B C ATOM 1675 CD1 TYR B 157 67.800 20.430 150.837 1.00 22.81 B C ATOM 1676 CE1 TYR B 157 67.891 21.233 149.703 1.00 24.82 B C ATOM 1677 CD2 TYR B 157 67.567 18.492 149.451 1.00 24.09 B C ATOM 1678 CE2 TYR B 157 67.658 19.285 148.313 1.00 24.05 B C ATOM 1679 CZ TYR B 157 67.820 20.652 148.445 1.00 25.74 B C ATOM 1680 OH TYR E 157 67.919 21.438 147.319 1.00 32.12 B O ATOM 1681 C TYR B 157 65.991 17.297 153.735 1.00 27.77 B C ATOM 1682 O TYR B 157 66.644 16.254 153.696 1.00 28.36 B O ATOM 1683 N SER B 158 65.162 17.576 154.731 1.00 29.96 B N ATOM 1684 CA SER B 158 65.006 16.641 155.834 1.00 32.14 B C ATOM 1685 CB SER B 158 65.751 17.144 157.077 1.00 32.84 B C ATOM 1686 OG SER B 158 65.274 18.414 157.490 1.00 34.79 B O ATOM 1687 C SER B 158 63.549 16.412 156.178 1.00 33.22 B C ATOM 1688 O SER B 158 62.667 17.155 155.750 1.00 29.83 B O ATOM 1689 N ARG B 159 63.319 15.376 156.973 1.00 37.03 B N ATOM 1690 CA ARO B 159 61.990 14.999 157.418 1.00 40.29 B C ATOM 1691 CB ARG B 159 62.071 13.676 158.176 1.00 46.56 B C ATOM 1692 CG ARG E 159 60.957 12.699 157.863 1.00 57.91 B C ATOM 1693 CD ARG B 159 61.049 11.467 158.757 1.00 64.70 B C ATOM 1694 NE ARG B 159 59.974 10.514 158.490 1.00 70.47 B N ATOM 1695 CZ ARG B 159 59.694 9.466 159.260 1.00 73.51 B C ATOM 1696 NE1 ARG B 159 58.698 8.651 158.937 1.00 74.22 B N ATOM 1697 NH2 ARG B 159 60.406 9.237 160.357 1.00 74.50 B N ATOM 1698 C ARG B 159 61.395 16.078 158.325 1.00 38.61 B C ATOM 1699 O ARG B 159 60.264 15.949 158.781 1.00 39.20 B O ATOM 1700 N ASP B 160 62.160 17.135 158.583 1.00 37.90 B N ATOM 1701 CA ASP B 160 61.707 18.233 159.438 1.00 36.97 B C ATOM 1702 CB ASP B 160 62.894 19.043 159.971 1.00 42.42 B C ATOM 1703 CG ASP B 160 63.908 18.195 160.698 1.00 46.87 B C ATOM 1704 OD1 ASP B 160 63.505 17.346 161.523 1.00 49.44 B O ATOM 1705 OD2 ASP B 160 65.116 18.393 160.451 1.00 50.63 B O ATOM 1706 C ASP B 160 60.784 19.198 158.706 1.00 33.52 B C ATOM 1707 O ASP B 160 60.165 20.065 159.326 1.00 33.69 B O ATOM 1708 N ALA B 161 60.706 19.065 157.389 1.00 29.73 B N ATOM 1709 CA ALA B 161 59.864 19.948 156.594 1.00 25.02 B C ATOM 1710 CB ALA B 161 60.019 19.620 155.116 1.00 24.48 B C ATOM 1711 C ALA B 161 58.408 19.808 157.005 1.00 22.73 B C ATOM 1712 O ALA B 161 57.983 18.743 157.453 1.00 18.59 B O ATOM 1713 N ASP B 162 57.644 20.886 156.865 1.00 20.01 B N ATOM 1714 CA ASP B 162 56.226 20.835 157.207 1.00 19.49 B C ATOM 1715 CB ASP B 162 55.625 22.240 157.298 1.00 17.17 B C ATOM 1716 CG ASP B 162 56.279 23.087 158.365 1.00 15.31 B C ATOM 1717 OD1 ASP B 162 56.422 22.601 159.505 1.00 16.45 B O ATOM 1718 OD2 ASP B 162 56.643 24.242 158.066 1.00 14.81 B O ATOM 1719 C ASP B 162 55.486 20.055 156.128 1.00 20.86 B C ATOM 1720 O ASP B 162 54.620 19.240 156.417 1.00 19.12 B O ATOM 1721 N ILE B 163 55.836 20.312 154.875 1.00 20.30 B N ATOM 1722 CA ILE B 163 55.183 19.646 153.760 1.00 17.16 B C ATOM 1723 CB ILE B 163 54.640 20.692 152.748 1.00 19.96 B C ATOM 1724 CO2 ILE B 163 54.032 19.995 151.530 1.00 16.75 B C ATOM 1725 CO1 ILE B 163 53.611 21.587 153.449 1.00 20.77 B C ATOM 1726 OD1 ILE B 163 53.139 22.769 152.625 1.00 16.61 B C ATOM 1727 C ILE B 163 56.138 18.694 153.058 1.00 15.84 B C ATOM 1728 O ILE B 163 57.096 19.114 152.411 1.00 16.45 B O ATOM 1729 N VAL B 164 55.883 17.405 153.207 1.00 13.42 B N ATOM 1730 CA VAL B 164 56.711 16.408 152.567 1.00 13.63 B C ATOM 1731 OB VAL B 164 56.977 15.221 153.498 1.00 13.46 B C ATOM 1732 CG1 VAL B 164 57.737 14.136 152.750 1.00 11.25 B C ATOM 1733 CG2 VAL B 164 57.773 15.694 154.713 1.00 12.79 B C ATOM 1734 C VAL B 164 55.991 15.939 151.310 1.00 14.94 B C ATOM 1735 O VAL B 164 54.826 15.535 151.358 1.00 15.76 B O ATOM 1736 N ILE B 165 56.698 16.015 150.187 1.00 13.79 B N ATOM 1737 CA ILE B 165 56.165 15.636 148.886 1.00 12.71 B C ATOM 1738 OB ILE B 165 56.472 16.714 147.857 1.00 14.97 B C ATOM 1739 CO2 ILE B 165 55.912 16.306 146.503 1.00 13.61 B C ATOM 1740 CO1 ILE B 165 55.919 18.059 148.348 1.00 13.19 B C ATOM 1741 CD1 LLE B 165 56.377 19.259 147.543 1.00 14.12 B C ATOM 1742 C ILE B 165 56.749 14.334 148.381 1.00 13.67 B C ATOM 1743 O ILE B 165 57.949 14.096 148.491 1.00 11.91 B O ATOM 1744 N GLN B 166 55.903 13.481 147.820 1.00 14.64 B N ATOM 1745 CA GLN B 166 56.400 12.230 147.291 1.00 17.38 B C ATOM 1746 CB GLN B 166 56.599 11.209 148.412 1.00 20.52 B C ATOM 1747 CG GLN B 166 55.328 10.614 148.956 1.00 28.99 B C ATOM 1748 CD GLN B 166 55.589 9.395 149.828 1.00 34.11 B C ATOM 1749 OB1 GLN B 166 55.972 8.329 149.334 1.00 34.45 B O ATOM 1750 NB2 GLN B 166 55.392 9.550 151.134 1.00 36.00 B N ATOM 1751 C GLN B 166 55.511 11.625 146.226 1.00 16.18 B C ATOM 1752 O QLN B 166 54.304 11.856 146.204 1.00 14.81 B O ATOM 1753 N PHE B 167 56.141 10.859 145.339 1.00 14.40 B N ATOM 1754 CA PHE B 167 55.463 10.147 144.274 1.00 13.46 B C ATOM 1755 CB PHE B 167 56.237 10.257 142.959 1.00 9.79 B C ATOM 1756 CG PHE B 167 56.265 11.642 142.386 1.00 11.55 B C ATOM 1757 CD1 PHE B 167 57.172 12.581 142.852 1.00 12.24 B C ATOM 1758 CD2 PHE B 167 55.371 12.012 141.388 1.00 12.04 B C ATOM 1759 CE1 PEE B 167 57.191 13.874 142.334 1.00 12.05 B C ATOM 1760 CE2 PHE B 167 55.379 13.306 140.865 1.00 11.98 B C ATOM 1761 CZ PHE B 167 56.288 14.237 141.338 1.00 13.47 B C ATOM 1762 C PHE B 167 55.414 8.685 144.681 1.00 14.78 B C ATOM 1763 O PHE B 167 56.389 8.160 145.202 1.00 16.19 B O ATOM 1764 N GLY B 168 54.283 8.028 144.446 1.00 16.63 B N ATOM 1765 CA GLY B 168 54.170 6.626 144.795 1.00 18.19 B C ATOM 1766 C GLY B 168 53.143 5.900 143.951 1.00 20.06 B C ATOM 1767 O GLY B 168 52.352 6.535 143.260 1.00 21.45 B O ATOM 1768 N VAL B 169 53.168 4.572 143.988 1.00 21.07 B N ATOM 1769 CA VAL B 169 52.206 3.764 143.247 1.00 22.74 B C ATOM 1770 CB VAL B 169 52.875 2.967 142.109 1.00 22.64 B C ATOM 1771 GG1 VAL B 169 53.593 3.913 141.170 1.00 22.95 B C ATOM 1772 CG2 VAL B 169 53.832 1.943 142.686 1.00 23.18 B C ATOM 1773 C VAL B 169 51.547 2.773 144.203 1.00 24.58 B C ATOM 1774 O VAL B 169 52.210 2.174 145.055 1.00 24.53 B O ATOM 1775 N ALA B 170 50.238 2.607 144.061 1.00 25.72 B N ATOM 1776 CA ALA B 170 49.498 1.690 144.912 1.00 25.50 B C ATOM 1777 CB ALA B 170 49.845 0.256 144.543 1.00 24.40 B C ATOM 1778 C ALA B 170 49.826 1.959 146.379 1.00 25.00 B C ATOM 1779 O ALA B 170 49.761 3.106 146.836 1.00 23.10 B O ATOM 1780 N GLU B 171 50.179 0.902 147.105 1.00 26.18 B N ATOM 1781 CA GLU B 171 50.521 1.002 148.523 1.00 30.44 B C ATOM 1782 CB GLU B 171 50.756 −0.391 149.113 1.00 37.69 B C ATOM 1783 CG GLU B 171 49.929 −1.502 148.484 1.00 50.32 B C ATOM 1784 CD GLU B 171 48.452 −1.388 148.800 1.00 56.96 B C ATOM 1785 OE1 GLU B 171 47.671 −2.226 148.296 1.00 59.68 B O ATOM 1786 OE2 GLU B 171 48.074 −0.464 149.555 1.00 61.18 B O ATOM 1787 C GLU B 171 51.810 1.802 148.647 1.00 28.21 B C ATOM 1788 O GLU B 171 52.839 1.399 148.108 1.00 26.23 B O ATOM 1789 N HIS B 172 51.776 2.922 149.360 1.00 26.31 B N ATOM 1790 CA HIS B 172 52.989 3.723 149.488 1.00 26.29 B C ATOM 1791 CB HIS B 172 52.935 4.898 148.500 1.00 21.05 B C ATOM 1792 CG HIS B 172 51.733 5.777 148.671 1.00 19.27 B C ATOM 1793 CD2 HIS B 172 51.536 6.874 149.438 1.00 17.23 B C ATOM 1794 ND1 HIS B 172 50.526 5.519 148.056 1.00 15.56 B N ATOM 1795 CR1 HiS B 172 49.638 6.416 148.441 1.00 14.96 B C ATOM 1796 NE2 HIS B 172 50.225 7.248 149.281 1.00 13.17 B N ATOM 1797 C HIS B 172 53.334 4.246 150.890 1.00 27.55 B C ATOM 1798 O HIS B 172 54.057 5.231 151.019 1.00 26.45 B O ATOM 1799 N GLY B 173 52.831 3.601 151.940 1.00 30.22 B N ATOM 1800 CA GLY B 173 53.154 4.070 153.280 1.00 32.63 B C ATOM 1801 C GLY B 173 51.972 4.307 154.198 1.00 35.23 B C ATOM 1802 O GLY B 173 51.827 3.621 155.209 1.00 39.12 B O ATOM 1803 N ASP B 174 51.138 5.289 153.875 1.00 33.34 B N ATOM 1804 CA ASP B 174 49.968 5.563 154.692 1.00 33.01 B C ATOM 1805 CB ASP B 174 49.343 6.899 154.299 1.00 34.56 B C ATOM 1806 CG ASP B 174 49.366 7.138 152.797 1.00 33.72 B C ATOM 1807 OD1 ASP B 174 49.119 6.191 152.023 1.00 30.99 B O ATOM 1808 OD2 ASP B 174 49.623 8.286 152.395 1.00 32.06 B O ATOM 1809 C ASP B 174 48.969 4.438 154.475 1.00 33.84 B C ATOM 1810 O ASP B 174 49.323 3.368 153.982 1.00 35.39 B O ATOM 1811 N GLY B 175 47.719 4.666 154.837 1.00 34.25 B N ATOM 1812 CA GLY B 175 46.732 3.620 154.641 1.00 36.75 B C ATOM 1813 C GLY B 175 45.836 3.952 153.474 1.00 35.04 B C ATOM 1814 O GLY B 175 44.705 3.478 153.390 1.00 37.61 B O ATOM 1815 N TYR B 176 46.359 4.768 152.566 1.00 33.73 B N ATOM 1816 CA TYR B 176 45.597 5.200 151.409 1.00 32.53 B C ATOM 1817 CB TYR B 176 45.285 6.690 151.545 1.00 35.60 B C ATOM 1818 CO TYR B 176 44.636 7.044 152.867 1.00 40.89 B C ATOM 1819 CD1 TYR B 176 45.334 6.907 154.070 1.00 43.33 B C ATOM 1820 CE1 TYR B 176 44.736 7.204 155.290 1.00 43.67 B C ATOM 1821 CD2 TYR B 176 43.318 7.492 152.922 1.00 42.09 B C ATOM 1822 CE2 TYR B 176 42.711 7.794 154.140 1.00 42.63 B C ATOM 1823 CZ TYR B 176 43.426 7.647 155.317 1.00 43.63 B C ATOM 1824 OH TYR B 176 42.835 7.947 156.519 1.00 45.29 B O ATOM 1825 C TYR B 176 46.309 4.931 150.089 1.00 30.01 B C ATOM 1826 O TYR B 176 46.907 5.825 149.303 1.00 29.44 B O ATOM 1827 N PRO B 177 46.255 3.686 149.604 1.00 29.94 B N ATOM 1828 CD PRO B 177 45.706 2.475 150.238 1.00 28.60 B C ATOM 1829 CA PRO B 177 46.918 3.366 148.335 1.00 28.82 B C ATOM 1830 CB PRO B 177 46.838 1.843 148.280 1.00 29.21 B C ATOM 1831 CG PRO B 177 45.590 1.533 149.067 1.00 30.96 B C ATOM 1832 C PRO B 177 46.253 4.029 147.128 1.00 28.62 B C ATOM 1833 O PRO B 177 45.070 4.372 147.167 1.00 30.61 B O ATOM 1834 N PHE B 178 47.023 4.225 146.062 1.00 26.71 B N ATOM 1835 CA PHE B 178 46.475 4.825 144.851 1.00 26.70 B C ATOM 1836 CB PHE B 178 47.568 5.547 144.055 1.00 22.42 B C ATOM 1837 CG PHE B 178 48.019 6.842 144.687 1.00 17.95 B C ATOM 1838 CD1 PHE B 178 47.108 7.871 144.919 1.00 16.47 B C ATOM 1839 CD2 PHE B 178 49.349 7.029 145.058 1.00 17.30 B C ATOM 1840 CE1 PHE B 178 47.511 9.069 145.511 1.00 14.31 B C ATOM 1841 CE2 PHE B 178 49.765 8.221 145.650 1.00 14.81 B C ATOM 1842 CZ PHE B 178 48.842 9.245 145.877 1.00 16.31 B C ATOM 1843 C PHE B 178 45.810 3.733 144.017 1.00 26.77 B C ATOM 1844 O PHE B 178 46.020 2.546 144.261 1.00 23.82 B O ATOM 1845 N ASP B 179 45.017 4.142 143.032 1.00 28.61 B N ATOM 1846 CA ASP B 179 44.259 3.209 142.203 1.00 29.98 B C ATOM 1847 CB ASP B 179 42.808 3.674 142.164 1.00 29.97 B C ATOM 1848 CG ASP B 179 42.698 5.131 141.810 1.00 30.41 B C ATOM 1849 OD1 ASP B 179 43.709 5.661 141.331 1.00 35.31 B O ATOM 1850 OD2 ASP B 179 41.631 5.750 141.995 1.00 33.11 B O ATOM 1851 C ASP B 179 44.731 2.976 140.768 1.00 30.43 B C ATOM 1852 O ASP B 179 43.924 2.646 139.909 1.00 30.49 B O ATOM 1853 N GLY B 180 46.020 3.128 140.499 1.00 30.89 B N ATOM 1854 CA GLY B 180 46.493 2.905 139.146 1.00 29.05 B C ATOM 1855 C GLY B 180 46.142 4.064 138.237 1.00 29.44 B C ATOM 1856 O GLY B 180 45.789 5.131 138.723 1.00 25.58 B O ATOM 1857 N LYS B 181 46.217 3.849 136.925 1.00 29.06 B N ATOM 1858 CA LYS B 181 45.936 4.895 135.943 1.00 30.26 B C ATOM 1859 CB LYS B 181 46.100 4.322 134.535 1.00 33.27 B C ATOM 1860 CG LYS B 181 45.992 5.346 133.426 1.00 36.93 B C ATOM 1861 CD LYS B 181 46.258 4.704 132.077 1.00 41.28 B C ATOM 1862 CE LYS B 181 46.044 5.691 130.936 1.00 44.88 B C ATOM 1863 NZ LYS B 181 44.634 6.176 130.859 1.00 43.95 B N ATOM 1864 C LYS B 181 44.565 5.565 136.087 1.00 28.94 B C ATOM 1865 O LYS B 181 43.545 4.901 136.239 1.00 30.47 B O ATOM 1866 N ASP B 182 44.561 6.892 136.034 1.00 29.99 B N ATOM 1867 CA ASP B 182 43.347 7.692 136.166 1.00 30.47 B C ATOM 1868 CB ASP B 182 42.367 7.376 135.035 1.00 35.39 B C ATOM 1869 CG ASP B 182 42.877 7.826 133.684 1.00 38.40 B C ATOM 1870 OD1 ASP B 182 43.081 9.045 133.491 1.00 39.28 B O ATOM 1871 OD2 ASP B 182 43.078 6.954 132.814 1.00 42.49 B O ATOM 1872 C ASP B 182 42.642 7.509 137.506 1.00 31.65 B C ATOM 1873 O ASP B 182 43.099 6.765 138.363 1.00 32.44 B O ATOM 1874 N GLY B 183 41.509 8.181 137.670 1.00 29.41 B N ATOM 1875 CA GLY B 183 40.774 8.091 138.912 1.00 27.84 B C ATOM 1876 C GLY B 183 41.335 9.123 139.864 1.00 27.88 B C ATOM 1877 O GLY B 183 41.355 10.310 139.549 1.00 29.24 B O ATOM 1878 N LEU B 184 41.792 8.678 141.030 1.00 27.15 B N ATOM 1879 CA LEU B 184 42.376 9.585 142.015 1.00 25.82 B C ATOM 1880 CB LEU B 184 42.493 8.878 143.359 1.00 27.95 B C ATOM 1881 CG LEU B 184 42.940 9.772 144.507 1.00 30.41 B C ATOM 1882 CD1 LEU B 184 41.855 10.797 144.779 1.00 28.19 B C ATOM 1883 CD2 LEU B 184 43.205 8.927 145.746 1.00 34.06 B C ATOM 1884 C LEU B 184 43.771 9.971 141.520 1.00 22.60 B C ATOM 1885 O LEU B 184 44.593 9.106 141.265 1.00 17.85 B O ATOM 1886 N LEU B 185 44.047 11.262 141.397 1.00 22.16 B N ATOM 1887 CA LEU B 185 45.346 11.700 140.884 1.00 22.33 B C ATOM 1888 CB LEU B 185 45.177 13.002 140.095 1.00 19.27 B C ATOM 1889 CG LEU B 185 44.127 12.970 138.979 1.00 20.81 B C ATOM 1890 CD1 LEU B 185 44.110 14.305 138.252 1.00 12.81 B C ATOM 1891 CD2 LEU B 185 44.425 11.823 138.013 1.00 17.71 B C ATOM 1892 C LEU B 185 46.400 11.897 141.965 1.00 23.14 B C ATOM 1893 O LEU B 185 47.593 11.658 141.749 1.00 22.98 B O ATOM 1894 N ALA B 186 45.948 12.331 143.131 1.00 23.03 B N ATOM 1895 CA ALA B 186 46.830 12.585 144.255 1.00 22.63 B C ATOM 1896 CB ALA B 186 47.717 13.768 143.942 1.00 21.82 B C ATOM 1897 C ALA B 186 45.974 12.896 145.472 1.00 23.10 B C ATOM 1898 O ALA B 186 44.751 12.932 145.378 1.00 25.16 B O ATOM 1899 N HIS B 187 46.622 13.104 146.613 1.00 22.01 B N ATOM 1900 CA HIS B 187 45.927 13.458 147.840 1.00 21.61 B C ATOM 1901 CB HIS B 187 45.218 12.237 148.451 1.00 19.44 B C ATOM 1902 CG HIS B 187 46.126 11.110 148.838 1.00 21.62 B C ATOM 1903 CD2 HIS B 187 47.343 11.101 149.434 1.00 23.01 B C ATOM 1904 ND1 HIS B 187 45.771 9.787 148.673 1.00 20.29 B N ATOM 1905 CE1 HiS B 187 46.730 9.013 149.151 1.00 20.79 B C ATOM 1906 NE2 HIS B 187 47.695 9.786 149.619 1.00 19.38 B N ATOM 1907 C HIS B 187 46.898 14.097 148.822 1.00 22.17 B C ATOM 1908 O HIS B 187 48.086 13.786 148.818 1.00 21.16 B O ATOM 1909 N ALA B 188 46.386 15.015 149.637 1.00 19.90 B N ATOM 1910 CA ALA B 188 47.191 15.727 150.615 1.00 21.04 B C ATOM 1911 CB ALA B 188 47.386 17.165 150.169 1.00 16.20 B C ATOM 1912 C ALA B 188 46.511 15.689 151.981 1.00 24.29 B C ATOM 1913 O ALA B 188 45.342 15.313 152.091 1.00 23.00 B 0 ATOM 1914 N PHE B 189 47.248 16.076 153.020 1.00 25.22 B N ATOM 1915 CA PHE B 189 46.712 16.081 154.373 1.00 23.69 B C ATOM 1916 CB PHE B 189 47.532 15.162 155.290 1.00 23.93 B C ATOM 1917 CG PHE B 189 47.565 13.731 154.839 1.00 26.85 B C ATOM 1918 CD1 PUE B 189 48.483 13.308 153.881 1.00 29.60 B C ATOM 1919 CD2 PHE B 189 46.668 12.806 155.358 1.00 27.63 B C ATOM 1920 CE1 PHE B 189 48.510 11.984 153.447 1.00 27.95 B C ATOM 1921 CE2 PHE B 189 46.685 11.480 154.930 1.00 29.13 B C ATOM 1922 CZ PHE B 189 47.609 11.069 153.972 1.00 29.53 B C ATOM 1923 C PHE B 189 46.712 17.491 154.932 1.00 24.15 B C ATOM 1924 O PHE B 189 47.600 18.286 154.632 1.00 23.64 B O ATOM 1925 N PRO B 190 45.703 17.818 155.761 1.00 25.45 B N ATOM 1926 CD PRO B 190 44.626 16.901 156.165 1.00 24.82 B C ATOM 1927 CA PRO B 190 45.535 19.135 156.399 1.00 23.84 B C ATOM 1928 CB PRO B 190 44.211 18.998 157.151 1.00 23.85 B C ATOM 1929 CG PRO B 190 43.517 17.859 156.470 1.00 27.72 B C ATOM 1930 C PRO B 190 46.693 19.452 157.355 1.00 24.12 B C ATOM 1931 O PRO B 190 47.364 18.544 157.851 1.00 24.59 B O ATOM 1932 N PRO B 191 46.929 20.745 157.633 1.00 23.67 B N ATOM 1933 CD PRO B 191 46.130 21.889 157.160 1.00 22.01 B C ATOM 1934 CA PRO B 191 48.005 21.193 158.527 1.00 24.52 B C ATOM 1935 CB PRO B 191 47.668 22.660 158.756 1.00 23.21 B C ATOM 1936 CG PRO B 191 47.036 23.056 157.463 1.00 23.95 B C ATOM 1937 C PRO B 191 48.077 20.402 159.834 1.00 26.78 B C ATOM 1938 O PRO B 191 47.054 19.982 160.374 1.00 27.80 B O ATOM 1939 N GLY B 192 49.294 20.207 160.334 1.00 26.68 B N ATOM 1940 CA GLY B 192 49.490 19.459 161.563 1.00 25.28 B C ATOM 1941 C GLY B 192 50.851 18.786 161.573 1.00 26.25 B C ATOM 1942 O GLY B 192 51.653 19.026 160.671 1.00 27.65 B O ATOM 1943 N PRO B 193 51.145 17.935 162.574 1.00 26.70 B N ATOM 1944 CD PRO B 193 50.356 17.760 163.808 1.00 23.89 B C ATOM 1945 CA PRO B 193 52.428 17.233 162.685 1.00 26.43 B C ATOM 1946 CB PRO B 193 52.572 17.049 164.189 1.00 26.13 B C ATOM 1947 CG PRO B 193 51.173 16.742 164.588 1.00 24.53 B C ATOM 1948 C PRO B 193 52.463 15.901 161.947 1.00 25.56 B C ATOM 1949 O PRO B 193 51.423 15.356 161.592 1.00 28.95 B O ATOM 1950 N GLY B 194 53.665 15.379 161.721 1.00 24.12 B N ATOM 1951 CA GLY B 194 53.803 14.100 161.046 1.00 22.38 B C ATOM 1952 C GLY B 194 53.338 14.098 159.605 1.00 23.14 B C ATOM 1953 O GLY B 194 53.602 15.036 158.868 1.00 21.24 B O ATOM 1954 N ILE B 195 52.633 13.048 159.202 1.00 24.37 B N ATOM 1955 CA ILE B 195 52.147 12.941 157.832 1.00 26.26 B C ATOM 1956 CB ILE B 195 51.440 11.590 157.613 1.00 27.60 B C ATOM 1957 CG2 ILE B 195 50.131 11.561 158.386 1.00 27.08 B C ATOM 1958 CG1 ILE B 195 51.200 11.365 156.119 1.00 29.76 B C ATOM 1959 CD1 ILE B 195 50.620 10.012 155.789 1.00 31.30 B C ATOM 1960 C ILE B 195 51.194 14.085 157.479 1.00 26.36 B C ATOM 1961 O ILE B 195 50.921 14.343 156.309 1.00 27.06 B O ATOM 1962 N GLN B 196 50.704 14.781 158.498 1.00 26.62 B N ATOM 1963 CA GLN B 196 49.790 15.901 158.298 1.00 26.46 B C ATOM 1964 CE GLN B 196 49.359 16.457 159.654 1.00 29.46 B C ATOM 1965 CG GLN B 196 47.864 16.383 159.914 1.00 38.14 B C ATOM 1966 CD GLN B 196 47.323 14.967 159.860 1.00 41.94 B C ATOM 1967 OE1 GLN B 196 46.116 14.751 159.940 1.00 44.27 B O ATOM 1968 NE2 GLN B 196 48.215 13.993 159.727 1.00 46.11 B N ATOM 1969 C GLN B 196 50.459 16.998 157.482 1.00 23.79 B C ATOM 1970 O GLN B 196 51.576 17.367 157.768 1.00 25.59 B O ATOM 1971 N GLY B 197 49.774 17.524 156.472 1.00 23.38 B N ATOM 1972 CA GLY B 197 50.364 18.568 155.650 1.00 18.35 B C ATOM 1973 C GLY B 197 51.149 18.047 154.450 1.00 20.05 B C ATOM 1974 O GLY B 197 51.606 18.835 153.619 1.00 21.28 B O ATOM 1975 N ASP B 198 51.308 16.727 154.354 1.00 18.69 B N ATOM 1976 CA ASP B 198 52.049 16.115 153.253 1.00 18.67 B C ATOM 1977 CB ASP B 198 52.557 14.730 153.668 1.00 17.24 B C ATOM 1978 CG ASP B 198 53.613 14.794 154.764 1.00 19.44 B C ATOM 1979 OD1 ASP B 198 53.978 15.912 155.160 1.00 14.37 B O ATOM 1980 OD2 ASP B 198 54.080 13.730 155.220 1.00 16.31 B O ATOM 1981 C ASP B 198 51.203 15.996 151.974 1.00 20.96 B C ATOM 1982 O ASP B 198 49.971 16.042 152.029 1.00 21.22 B O ATOM 1983 N ALA B 199 51.872 15.836 150.831 1.00 18.26 B N ATOM 1984 CA ALA B 199 51.197 15.722 149.536 1.00 17.33 B C ATOM 1985 CB ALA B 199 51.326 17.027 148.771 1.00 16.82 B C ATOM 1986 C ALA B 199 51.803 14.586 148.728 1.00 18.72 B C ATOM 1987 O ALA B 199 53.004 14.569 148.483 1.00 20.07 B O ATOM 1988 N HIS B 200 50.968 13.639 148.314 1.00 17.89 B N ATOM 1989 CA HIS B 200 51.424 12.481 147.555 1.00 15.98 B C ATOM 1990 CB HIS B 200 51.092 11.215 148.334 1.00 17.39 B C ATOM 1991 CG HIS B 200 51.623 11.212 149.736 1.00 20.36 B C ATOM 1992 CD2 HIS B 200 52.599 11.944 150.325 1.00 17.40 B C ATOM 1993 ND1 HIS B 200 51.160 10.349 150.704 1.00 18.51 B N ATOM 1994 CB1 HIS B 200 51.827 10.546 151.826 1.00 17.19 B C ATOM 1995 NE2 HIS B 200 52.706 11.508 151.623 1.00 17.14 B N ATOM 1996 C HIS B 200 50.786 12.427 146.168 1.00 18.64 B C ATOM 1997 O HIS B 200 49.591 12.668 146.016 1.00 18.44 B O ATOM 1998 N PHE B 201 51.594 12.105 145.160 1.00 19.00 B N ATOM 1999 CA PHE B 201 51.128 12.046 143.776 1.00 15.37 B C ATOM 2000 CB PHE B 201 51.929 13.027 142.912 1.00 16.11 B C ATOM 2001 CG PHE B 201 51.907 14.444 143.421 1.00 14.27 B C ATOM 2002 CD1 PHE B 201 52.747 14.840 144.459 1.00 15.41 B C ATOM 2003 CD2 PHE B 201 51.017 15.374 142.887 1.00 13.45 B C ATOM 2004 GE1 PHE B 201 52.704 16.143 144.961 1.00 15.16 B C ATOM 2005 CE2 PHE B 201 50.962 16.685 143.380 1.00 14.52 B C ATOM 2006 CZ PHE B 201 51.806 17.071 144.418 1.00 14.98 B C ATOM 2007 C PHE B 201 51.227 10.650 143.185 1.00 15.36 B C ATOM 2008 O PHE B 201 52.257 9.993 143.293 1.00 15.05 B O ATOM 2009 N ASP B 202 50.144 10.204 142.555 1.00 16.99 B N ATOM 2010 CA ASP B 202 50.094 8.877 141.941 1.00 18.47 B C ATOM 2011 CB ASP B 202 48.660 8.502 141.583 1.00 16.97 B C ATOM 2012 CG ASP B 202 48.546 7.080 141.116 1.00 17.69 B C ATOM 2013 OD1 ASP B 202 49.567 6.496 140.725 1.00 24.22 B O ATOM 2014 OD2 ASP B 202 47.442 6.530 141.132 1.00 22.67 B O ATOM 2015 C ASP B 202 50.944 8.843 140.673 1.00 17.99 B C ATOM 2016 O ASP B 202 50.604 9.460 139.670 1.00 16.40 B O ATOM 2017 N ASP B 203 52.039 8.101 140.722 1.00 18.18 B N ATOM 2018 CA ASP B 203 52.943 8.020 139.593 1.00 19.10 B C ATOM 2019 CB ASP B 203 54.360 7.745 140.098 1.00 18.63 B C ATOM 2020 CG ASP B 203 55.424 8.234 139.147 1.00 21.55 B C ATOM 2021 OD1 ASP B 203 55.153 9.165 138.359 1.00 22.68 B O ATOM 2022 OD2 ASP B 203 56.546 7.700 139.204 1.00 24.38 B O ATOM 2023 C ASP B 203 52.522 6.977 138.560 1.00 22.02 B C ATOM 2024 O ASP B 203 53.328 6.553 137.739 1.00 22.79 B O ATOM 2025 N ASP B 204 51.274 6.529 138.627 1.00 21.73 B N ATOM 2026 CA ASP B 204 50.772 5.589 137.631 1.00 20.62 B C ATOM 2027 CB ASP B 204 49.729 4.635 138.212 1.00 19.80 B C ATOM 2028 CC ASP B 204 50.304 3.270 138.551 1.00 22.45 B C ATOM 2029 OD1 ASP B 204 51.334 2.884 137.963 1.00 20.45 B O ATOM 2030 OD2 ASP B 204 49.709 2.571 139.399 1.00 23.05 B O ATOM 2031 C ASP B 204 50.123 6.478 136.570 1.00 20.79 B C ATOM 2032 O ASP B 204 49.739 6.016 135.504 1.00 23.31 B O ATOM 2033 N GLU B 205 50.008 7.763 136.890 1.00 18.69 B N ATOM 2034 CA GLU B 205 49.441 8.755 135.987 1.00 20.13 B C ATOM 2035 CB GLU B 205 48.874 9.931 136.778 1.00 20.83 B C ATOM 2036 CG GLU B 205 47.935 9.526 137.894 1.00 29.96 B C ATOM 2037 CD GLU B 205 46.627 8.986 137.377 1.00 33.57 B C ATOM 2038 OE1 GLU B 205 46.617 8.360 136.293 1.00 36.59 B O ATOM 2039 OE2 GLU B 205 45.607 9.185 138.060 1.00 40.04 B O ATOM 2040 C GLU B 205 50.560 9.285 135.099 1.00 21.01 B C ATOM 2041 O GLU B 205 51.725 9.238 135.477 1.00 19.13 B O ATOM 2042 N LEU B 206 50.207 9.795 133.924 1.00 18.61 B N ATOM 2043 CA LEU B 206 51.204 10.366 133.026 1.00 17.96 B C ATOM 2044 CB LEU B 206 50.758 10.242 131.568 1.00 18.74 B C ATOM 2045 CG LEU B 206 51.617 10.985 130.532 1.00 19.98 B C ATOM 2046 CD1 LEU B 206 53.062 10.519 130.627 1.00 18.61 B C ATOM 2047 CD2 LEU B 206 51.064 10.740 129.131 1.00 17.02 B C ATOM 2048 C LEU B 206 51.312 11.837 133.399 1.00 18.42 B C ATOM 2049 O LEU B 206 50.379 12.603 133.160 1.00 18.49 B O ATOM 2050 N TRP B 207 52.434 12.230 133.998 1.00 17.94 B N ATOM 2051 CA TRP B 207 52.618 13.622 134.401 1.00 16.68 B C ATOM 2052 CB TRP B 207 53.454 13.723 135.694 1.00 15.77 B C ATOM 2053 CO TRP B 207 52.752 13.143 136.870 1.00 14.61 B C ATOM 2054 CD2 TRP B 207 51.546 13.636 137.469 1.00 14.73 B C ATOM 2055 CE2 TRP B 207 51.165 12.708 138.464 1.00 14.79 B C ATOM 2056 CE3 TRP B 207 50.744 14.769 137.255 1.00 16.70 B C ATOM 2057 CD1 TRP B 207 53.051 11.979 137.511 1.00 13.93 B C ATOM 2058 NE1 TRP B 207 52.101 11.708 138.467 1.00 15.76 B N ATOM 2059 CZ2 TRP B 207 50.012 12.876 139.248 1.00 13.38 B C ATOM 2060 CZ3 TRP B 207 49.591 14.935 138.034 1.00 13.30 B C ATOM 2061 CH2 TRP B 207 49.241 13.990 139.016 1.00 13.83 B C ATOM 2062 C TRY B 207 53.267 14.435 133.299 1.00 16.25 B C ATOM 2063 O TRP B 207 54.230 14.003 132.665 1.00 14.91 B O ATOM 2064 N SER B 208 52.731 15.630 133.092 1.00 16.82 B N ATOM 2065 CA SER B 208 53.218 16.521 132.061 1.00 15.97 B C ATOM 2066 CB SER B 208 52.497 16.187 130.747 1.00 16.80 B C ATOM 2067 OG SER B 208 53.111 16.799 129.634 1.00 12.64 B O ATOM 2068 C SER B 208 52.924 17.953 132.496 1.00 17.15 B C ATOM 2069 O SER B 208 52.677 18.207 133.676 1.00 20.26 B O ATOM 2070 N LEU B 209 52.954 18.881 131.543 1.00 15.88 B N ATOM 2071 CA LEU B 209 52.680 20.294 131.800 1.00 15.39 B C ATOM 2072 CB LEU B 209 53.972 21.049 132.105 1.00 12.60 B C ATOM 2073 CG LEU B 209 54.144 20.758 133.401 1.00 16.29 B C ATOM 2074 CD1 LEU B 209 56.029 21.560 133.386 1.00 12.54 B C ATOM 2075 CD2 LEU B 209 53.904 21.118 134.638 1.00 12.78 B C ATOM 2076 C LEU B 209 52.044 20.901 130.558 1.00 16.86 B C ATOM 2077 O LEU B 209 52.335 20.471 129.453 1.00 16.65 B O ATOM 2078 N GLY B 210 51.181 21.898 130.739 1.00 20.56 B N ATOM 2079 CA GLY B 210 50.545 22.557 129.602 1.00 20.23 B C ATOM 2080 C GLY B 210 49.475 21.767 128.864 1.00 21.25 B C ATOM 2081 O GLY B 210 48.885 20.835 129.409 1.00 21.72 B O ATOM 2082 N LYS B 211 49.207 22.158 127.621 1.00 20.99 B N ATOM 2083 CA LYS B 211 48.217 21.473 126.795 l.00 21.58 B C ATOM 2084 CB LYS B 211 47.879 22.314 125.560 1.00 22.10 B C ATOM 2085 CG LYS B 211 47.094 23.564 125.878 1.00 24.12 B C ATOM 2086 CD LYS B 211 46.828 24.410 124.647 1.00 27.19 B C ATOM 2087 CE LYS B 211 48.099 25.058 124.149 1.00 30.98 B C ATOM 2088 NZ LYS B 211 47.812 26.127 123.147 1.00 36.83 B N ATOM 2089 C LYS B 211 48.804 20.142 126.355 1.00 22.13 B C ATOM 2090 O LYS B 211 50.029 19.997 126.286 1.00 23.20 B O ATOM 2091 N GLY B 212 47.940 19.180 126.044 1.00 18.79 B N ATOM 2092 CA GLY B 212 48.420 17.877 125.623 1.00 17.78 B C ATOM 2093 C GLY B 212 47.925 16.758 126.521 1.00 18.87 B C ATOM 2094 O GLY B 212 47.238 17.010 127.515 1.00 19.58 B O ATOM 2095 N GLN B 391 48.268 15.519 126.181 1.00 19.71 B N ATOM 2096 CA GLN B 391 47.828 14.384 126.978 1.00 24.27 B C ATOM 2097 CB GLN B 391 48.024 13.073 126.200 1.00 26.88 B C ATOM 2098 CG GLN B 391 49.371 12.436 126.354 1.00 36.19 B C ATOM 2099 CD GLN B 391 50.489 13.421 126.157 1.00 42.59 B C ATOM 2100 OE1 GLN B 391 50.568 14.090 125.131 1.00 51.17 B O ATOM 2101 NE2 GLN B 391 51.368 13.520 127.144 1.00 50.82 B N ATOM 2102 C GLN B 391 48.582 14.369 128.311 1.00 22.67 B C ATOM 2103 O GLN B 391 49.614 15.024 128.456 1.00 19.97 B O ATOM 2104 N GLY B 392 48.050 13.635 129.284 1.00 22.31 B N ATOM 2105 CA GLY B 392 48.672 13.586 130.592 1.00 20.72 B C ATOM 2106 C GLY B 392 48.050 14.651 131.473 1.00 19.93 B C ATOM 2107 O GLY B 392 47.238 15.452 131.010 1.00 20.51 B O ATOM 2108 N TYR B 393 48.433 14.672 132.744 1.00 20.46 B N ATOM 2109 CA TYR B 393 47.896 15.643 133.692 1.00 18.29 B C ATOM 2110 CB TYR B 393 47.421 14.924 134.962 1.00 20.08 B C ATOM 2111 CG TYR B 393 46.248 13.989 134.746 1.00 16.50 B C ATOM 2112 CD1 TYR B 393 44.957 14.490 134.602 1.00 17.97 B C ATOM 2113 CB1 TYR B 393 43.871 13.647 134.397 1.00 16.85 B C ATOM 2114 CD2 TYR B 393 46.429 12.610 134.675 1.00 18.06 B C ATOM 2115 CE2 TYR B 393 45.342 11.747 134.467 1.00 17.10 B C ATOM 2116 CZ TYR B 393 44.064 12.281 134.329 1.00 18.56 B C ATOM 2117 OH TYR B 393 42.974 11.463 134.100 1.00 18.94 B O ATOM 2118 C TYR B 393 48.964 16.653 134.050 1.00 17.76 B C ATOM 2119 O TYR B 393 50.138 16.304 134.130 1.00 22.05 B O ATOM 2120 N SER B 394 48.560 17.901 134.271 1.00 17.69 B N ATOM 2121 CA SER B 394 49.505 18.955 134.627 1.00 18.43 B C ATOM 2122 CB SER B 394 48.864 20.331 134.464 1.00 15.87 B C ATOM 2123 OG SER B 394 49.799 21.357 134.756 1.00 17.63 B O ATOM 2124 C SER B 394 49.974 18.806 136.066 1.00 19.32 B C ATOM 2125 O SER B 394 49.185 18.953 136.997 1.00 23.73 B O ATOM 2126 N LEU B 395 51.253 18.512 136.255 1.00 18.56 B N ATOM 2127 CA LEU B 395 51.785 18.373 137.604 1.00 17.72 B C ATOM 2128 CB LEU B 395 53.265 17.972 137.556 1.00 16.48 B C ATOM 2129 CG LEU B 395 53.993 17.751 138.889 1.00 15.25 B C ATOM 2130 CD1 LEU B 395 53.311 16.631 139.670 1.00 13.74 B C ATOM 2131 CD2 LEU B 395 55.457 17.409 138.628 1.00 10.40 B C ATOM 2132 C LEU B 395 51.624 19.710 138.329 1.00 18.62 B C ATOM 2133 O LEU B 395 51.285 19.746 139.507 1.00 19.25 B O ATOM 2134 N PHE B 396 51.853 20.803 137.605 1.00 16.65 B N ATOM 2135 CA PHE B 396 51.741 22.152 138.152 1.00 17.42 B C ATOM 2136 CB PHE B 396 52.035 23.181 137.057 1.00 16.61 B C ATOM 2137 CG PHE B 396 51.661 24.592 137.421 1.00 17.86 B C ATOM 2138 CD1 PUB B 396 52.306 25.261 138.456 1.00 17.66 B C ATOM 2139 CD2 PHE B 396 50.666 25.259 136.714 1.00 19.99 B C ATOM 2140 CE1 PHE B 396 51.966 26.580 138.782 1.00 17.56 B C ATOM 2141 CE2 PUB B 396 50.319 26.573 137.030 1.00 20.09 B C ATOM 2142 CZ PHE B 396 50.974 27.236 138.070 1.00 19.48 B C ATOM 2143 C PUB B 396 50.369 22.429 138.749 1.00 20.69 B C ATOM 2144 O PUB B 396 50.257 22.821 139.916 1.00 20.46 B O ATOM 2145 N LEU B 397 49.329 22.234 137.942 1.00 20.63 B N ATOM 2146 CA LEU B 397 47.958 22.472 138.381 1.00 19.67 B C ATOM 2147 CB LEU B 397 46.985 22.340 137.201 1.00 19.64 B C ATOM 2148 CG LEU B 397 47.038 23.424 136.122 1.00 18.58 B C ATOM 2149 CD1 LEU B 397 45.965 23.156 135.086 1.00 45.91 B C ATOM 2150 CD2 LEU B 397 46.843 24.793 136.748 1.00 18.23 B C ATOM 2151 C LEU B 397 47.512 21.550 139.510 1.00 18.44 B C ATOM 2152 O LEU B 397 46.858 21.997 140.452 1.00 19.34 B O ATOM 2153 N VAL B 398 47.846 20.266 139.417 1.00 17.99 B N ATOM 2154 CA VAL B 398 47.464 19.326 140.466 1.00 19.04 B C ATOM 2155 CB VAt B 398 47.733 17.866 140.043 1.00 19.35 B C ATOM 2156 CG1 VAL B 398 47.353 16.905 141.173 1.00 15.55 B C ATOM 2157 CG2 VAL B 398 46.913 17.538 138.809 1.00 19.62 B C ATOM 2158 C VAL B 398 48.211 19.629 141.773 1.00 20.64 B C ATOM 2159 O VAL B 398 47.659 19.469 142.862 1.00 21.46 B O ATOM 2160 N ALA B 399 49.457 20.079 141.660 1.00 18.80 B N ATOM 2161 CA ALA B 399 50.254 20.411 142.834 1.00 21.04 B C ATOM 2162 CB ALA B 399 51.701 20.743 142.421 1.00 17.73 B C ATOM 2163 C ALA B 399 49.636 21.599 143.566 1.00 21.74 B C ATOM 2164 O ALA B 399 49.548 21.615 144.795 1.00 22.28 B O ATOM 2165 N ALA B 400 49.210 22.597 142.802 1.00 21.01 B N ATOM 2166 CA ALA B 400 48.611 23.787 143.378 1.00 20.55 B C ATOM 2167 CB ALA B 400 48.270 24.788 142.274 1.00 19.74 B C ATOM 2168 C ALA B 400 47.363 23.413 144.168 1.00 22.57 B C ATOM 2169 O ALA B 400 47.090 23.992 145.220 1.00 23.97 B O ATOM 2170 N HIS B 401 46.612 22.442 143.658 1.00 22.90 B N ATOM 2171 CA HIS B 401 45.397 21.980 144.321 1.00 23.48 B C ATOM 2172 CB HIS B 401 44.616 21.041 143.395 1.00 22.18 B C ATOM 2173 CG HIS B 401 43.328 20.544 143.976 1.00 23.80 B C ATOM 2174 CD2 HIS B 401 43.044 19.429 144.691 1.00 21.37 B C ATOM 2175 ND1 HIS B 401 42.138 21.230 143.847 1.00 23.81 B N ATOM 2176 CE1 HIS B 401 41.177 20.557 144.454 1.00 24.18 B C ATOM 2177 NE2 HIS B 401 41.699 19.461 144.976 1.00 21.29 B N ATOM 2178 C HIS B 401 45.763 21.246 145.615 1.00 24.30 B C ATOM 2179 O HIS B 401 45.192 21.519 146.673 1.00 24.53 B O ATOM 2180 N GLU B 402 46.714 20.317 145.529 1.00 23.82 B N ATOM 2181 CA GLU B 402 47.150 19.566 146.708 1.00 22.77 B C ATOM 2182 CB GLU B 402 48.217 18.530 146.341 1.00 22.35 B C ATOM 2183 CG GLU B 402 47.744 17.435 145.406 1.00 21.55 B C ATOM 2184 CD GLU B 402 46.298 17.071 145.636 1.00 21.21 B C ATOM 2185 OE1 GLU B 402 45.914 16.813 146.790 1.00 23.03 B O ATOM 2186 OE2 GLU B 402 45.539 17.043 144.654 1.00 26.51 B O ATOM 2187 C GLU B 402 47.710 20.486 147.785 1.00 22.14 B C ATOM 2188 O GLU B 402 47.431 20.301 148.966 1.00 24.45 B O ATOM 2189 N PHE B 403 48.504 21.473 147.382 1.00 22.87 B N ATOM 2190 CA PHE B 403 49.079 22.396 148.348 1.00 23.58 B C ATOM 2191 CB PHE B 403 50.124 23.308 147.688 1.00 20.83 B C ATOM 2192 CG PHE B 403 51.322 22.571 147.140 1.00 22.36 B C ATOM 2193 CD1 PHE B 403 51.587 21.252 147.518 1.00 20.84 B C ATOM 2194 CD2 PHE B 403 52.175 23.189 146.230 1.00 18.11 B C ATOM 2195 CE1 PHE B 403 52.682 20.560 146.989 1.00 21.54 B C ATOM 2196 CE2 PHE B 403 53.272 22.507 145.695 1.00 18.09 B C ATOM 2197 CZ PHE B 403 53.525 21.193 146.072 1.00 19.86 B C ATOM 2198 C PHE B 403 47.975 23.229 148.981 1.00 25.40 B C ATOM 2199 O PHE B 403 48.155 23.801 150.055 1.00 27.88 B O ATOM 2200 N GLY B 404 46.829 23.288 148.310 1.00 25.83 B N ATOM 2201 CA GLY B 404 45.703 24.038 148.833 1.00 25.16 B C ATOM 2202 C GLY B 404 45.208 23.328 150.076 1.00 25.03 B C ATOM 2203 O GLY B 404 44.922 23.953 151.096 1.00 24.69 B O ATOM 2204 N HIS B 405 45.110 22.008 149.980 1.00 23.03 B N ATOM 2205 CA HIS B 405 44.689 21.186 151.102 1.00 23.37 B C ATOM 2206 CB HIS B 405 44.537 19.731 150.668 1.00 21.33 B C ATOM 2207 CG HIS B 405 43.325 19.474 149.834 1.00 26.14 B C ATOM 2208 CD2 HIS B 405 43.164 18.781 148.683 1.00 23.33 B C ATOM 2209 ND1 HIS B 405 42.076 19.944 150.178 1.00 25.46 B N ATOM 2210 CE1 HIS B 405 41.198 19.551 149.274 1.00 26.71 B C ATOM 2211 NE2 HIS B 405 41.833 18.844 148.357 1.00 25.66 B N ATOM 2212 C HIS B 405 45.736 21.262 152.215 1.00 26.13 B C ATOM 2213 O HIS B 405 45.407 21.507 153.371 1.00 27.66 B O ATOM 2214 N ALA B 406 46.998 21.053 151.850 1.00 24.97 B N ATOM 2215 CA ALA B 406 48.099 21.082 152.802 1.00 25.23 B C ATOM 2216 CB ALA B 406 49.424 20.868 152.075 1.00 25.56 B C ATOM 2217 C ALA B 406 48.150 22.374 153.606 1.00 24.96 B C ATOM 2218 O ALA B 406 48.822 22.433 154.634 1.00 24.90 B O ATOM 2219 N LEU B 407 47.450 23.407 153.139 1.00 25.75 B N ATOM 2220 CA LEU B 407 47.424 24.683 153.849 1.00 26.02 B C ATOM 2221 CB LEU B 407 47.613 25.856 152.887 1.00 24.31 B C ATOM 2222 CG LEU B 407 48.951 25.959 152.146 1.00 27.21 B C ATOM 2223 CD1 LEU B 407 48.960 27.227 151.301 1.00 24.05 B C ATOM 2224 CD2 LEU B 407 50.110 25.979 153.132 1.00 25.82 B C ATOM 2225 C LEU B 407 46.121 24.869 154.627 1.00 27.45 B C ATOM 2226 O LEU B 407 45.947 25.868 155.323 1.00 28.27 B O ATOM 2227 N GLY B 408 45.208 23.910 154.504 1.00 27.89 B N ATOM 2228 CA GLY B 408 43.957 23.998 155.234 1.00 30.11 B C ATOM 2229 C GLY B 408 42.673 24.146 154.437 1.00 31.82 B C ATOM 2230 O GLY B 408 41.588 23.994 154.989 1.00 34.34 B O ATOM 2231 N LEU B 409 42.772 24.438 153.147 1.00 33.15 B N ATOM 2232 CA LEU B 409 41.575 24.601 152.325 1.00 32.57 B C ATOM 2233 CB LEU B 409 41.925 25.260 150.991 1.00 31.21 B C ATOM 2234 CG LEU B 409 42.400 26.711 151.009 1.00 32.82 B C ATOM 2235 CD1 LEU B 409 42.551 27.189 149.581 1.00 31.72 B C ATOM 2236 CD2 LEU B 409 41.397 27.589 151.747 1.00 33.90 B C ATOM 2237 C LEU B 409 40.826 23.305 152.034 1.00 33.31 B C ATOM 2238 O LEU B 409 41.427 22.250 151.850 1.00 32.51 B O ATOM 2239 N ASP B 410 39.500 23.396 152.003 1.00 35.18 B N ATOM 2240 CA ASP B 410 38.660 22.248 151.684 1.00 35.77 B C ATOM 2241 CB ASP B 410 37.422 22.186 152.595 1.00 42.82 B C ATOM 2242 CG ASP B 410 37.767 21.848 154.046 1.00 51.30 B C ATOM 2243 OD1 ASP B 410 38.706 21.050 154.273 1.00 53.65 B O ATOM 2244 OD2 ASP B 410 37.084 22.365 154.963 1.00 54.35 B O ATOM 2245 C ASP B 410 38.213 22.438 150.232 1.00 34.97 B C ATOM 2246 O ASP B 410 38.553 23.442 149.592 1.00 31.85 B O ATOM 2247 N HIS B 411 37.452 21.482 149.713 1.00 32.49 B N ATOM 2248 CA HIS B 411 36.967 21.565 148.342 1.00 33.78 B C ATOM 2249 CB HIS B 411 36.312 20.248 147.944 1.00 30.30 B C ATOM 2250 CG HIS B 411 37.294 19.186 147.573 1.00 29.54 B C ATOM 2251 CD2 HIS B 411 38.532 19.270 147.036 1.00 27.76 B C ATOM 2252 ND1 HIS B 411 37.039 17.843 147.741 1.00 28.79 B N ATOM 2253 GE1 HIS B 411 38.079 17.144 147.325 1.00 28.07 B C ATOM 2254 NE2 HIS B 411 38.998 17.986 146.892 1.00 31.97 B N ATOM 2255 C HIS B 411 35.985 22.704 148.128 1.00 35.95 B C ATOM 2256 O HIS B 411 35.224 23.062 149.028 1.00 38.94 B O ATOM 2257 N SER B 412 36.013 23.274 146.927 1.00 37.78 B N ATOM 2258 CA SER B 412 35.115 24.365 146.566 1.00 38.30 B C ATOM 2259 CB SER B 412 35.846 25.417 145.726 1.00 37.72 B C ATOM 2260 OG SER B 412 34.953 26.426 145.281 1.00 34.94 B O ATOM 2261 C SER B 412 33.957 23.800 145.763 1.00 39.44 B C ATOM 2262 O SER B 412 34.050 22.703 145.213 1.00 38.62 B O ATOM 2263 N SER B 413 32.862 24.553 145.715 1.00 41.65 B N ATOM 2264 CA SER B 413 31.672 24.149 144.973 1.00 43.35 B C ATOM 2265 CB SER B 413 30.414 24.431 145.806 1.00 43.75 B C ATOM 2266 OG SER B 413 30.416 25.759 146.311 1.00 45.44 B O ATOM 2267 C SER B 413 31.620 24.910 143.644 1.00 43.39 B C ATOM 2268 O SER B 413 30.789 24.627 142.782 1.00 43.76 B O ATOM 2269 N VAL B 414 32.520 25.878 143.495 1.00 43.36 B N ATOM 2270 CA VAL B 414 32.613 26.679 142.282 1.00 45.01 B C ATOM 2271 CB VAL B 414 33.330 28.015 142.569 1.00 43.92 B C ATOM 2272 CG1 VAL B 414 33.395 28.862 141.307 1.00 42.90 B C ATOM 2273 CG2 VAL B 414 32.606 28.761 143.691 1.00 42.04 B C ATOM 2274 C VAt B 414 33.418 25.873 141.257 1.00 49.61 B C ATOM 2275 O VAt B 414 34.639 25.731 141.384 1.00 50.35 B O ATOM 2276 N PRO B 415 32.739 25.326 140.231 1.00 53.34 B N ATOM 2277 CD PRO B 415 31.281 25.415 140.033 1.00 54.43 B C ATOM 2278 CA PRO B 415 33.348 24.518 139.166 1.00 54.30 B C ATOM 2279 CB PRO B 415 32.200 24.343 138.173 1.00 56.11 B C ATOM 2280 CG PRO B 415 31.014 24.261 139.078 1.00 55.46 B C ATOM 2281 C PRO B 415 34.614 25.060 138.505 1.00 52.96 B C ATOM 2282 O PRO B 415 35.396 24.287 137.955 1.00 54.37 B O ATOM 2283 N GLU B 416 34.818 26.373 138.544 1.00 50.37 B N ATOM 2284 CA GLU B 416 36.016 26.946 137.940 1.00 48.82 B C ATOM 2285 CB GLU B 416 35.662 28.135 137.041 1.00 53.26 B C ATOM 2286 CG GLU B 416 34.714 29.151 137.651 1.00 58.55 B C ATOM 2287 CD GLU B 416 33.266 28.900 137.270 1.00 61.82 B C ATOM 2288 OE1 GLU B 416 32.399 29.699 137.684 1.00 62.91 B O ATOM 2289 OE2 GLU B 416 32.994 27.907 136.556 1.00 63.31 B O ATOM 2290 C GLU B 416 37.059 27.369 138.971 1.00 45.83 B C ATOM 2291 O GLU B 416 38.023 28.060 138.646 1.00 45.77 B O ATOM 2292 N ALA B 417 36.859 26.964 140.220 1.00 40.82 B N ATOM 2293 CA ALA B 417 37.811 27.283 141.278 1.00 37.74 B C ATOM 2294 CB ALA B 417 37.105 27.337 142.632 1.00 33.86 B C ATOM 2295 C ALA B 417 38.867 26.181 141.281 1.00 36.14 B C ATOM 2296 O ALA B 417 38.561 25.018 140.984 1.00 34.99 B O ATOM 2297 N LEU B 418 40.107 26.543 141.605 1.00 34.03 B N ATOM 2298 CA LEU B 418 41.191 25.569 141.648 1.00 30.71 B C ATOM 2299 CB LEU B 418 42.502 26.248 142.048 1.00 31.54 B C ATOM 2300 CG LEU B 418 43.718 25.338 142.279 1.00 30.96 B C ATOM 2301 CD1 LEU B 418 44.048 24.554 141.013 1.00 28.41 B C ATOM 2302 CD2 LEU B 418 44.908 26.190 142.704 1.00 29.00 B C ATOM 2303 C LEU B 418 40.886 24.445 142.629 1.00 30.37 B C ATOM 2304 O LEU B 418 41.261 23.295 142.402 1.00 31.03 B O ATOM 2305 N MET B 419 40.197 24.772 143.719 1.00 29.50 B N ATOM 2306 CA MET B 419 39.871 23.764 144.717 1.00 30.42 B C ATOM 2307 CB MET B 419 39.657 24.418 146.085 1.00 31.33 B C ATOM 2308 CG MET B 419 40.933 24.997 146.691 1.00 31.92 B C ATOM 2309 SD MET B 419 42.360 23.881 146.543 1.00 33.33 B S ATOM 2310 CE MET B 419 41.836 22.484 147.532 1.00 27.72 B C ATOM 2311 C MET B 419 38.688 22.862 144.381 1.00 30.21 B C ATOM 2312 O MET B 419 38.301 22.021 145.193 1.00 30.07 B O ATOM 2313 N TYR B 420 38.119 23.026 143.190 1.00 31.40 B N ATOM 2314 CA TYR B 420 37.006 22.180 142.769 1.00 31.95 B C ATOM 2315 CB TYR B 420 36.550 22.570 141.356 1.00 36.57 B C ATOM 2316 CG TYR B 420 35.227 21.951 140.953 1.00 41.51 B C ATOM 2317 CD1 TYR B 420 34.035 22.330 141.577 1.00 43.15 B C ATOM 2318 CE1 TYR B 420 32.824 21.719 141.250 1.00 43.91 B C ATOM 2319 CD2 TYR B 420 35.173 20.947 139.986 1.00 42.71 B C ATOM 2320 CE2 TYR B 420 33.971 20.330 139.655 1.00 43.77 B C ATOM 2321 CZ TYR B 420 32.803 20.717 140.290 1.00 44.73 B C ATOM 2322 OH TYR B 420 34.628 20.080 139.969 1.00 45.83 B O ATOM 2323 C TYR B 420 37.558 20.749 142.790 1.00 31.80 B C ATOM 2324 O TYR B 420 38.658 20.498 142.310 1.00 35.03 B O ATOM 2325 N PRO B 421 36.797 19.792 143.340 1.00 31.81 B N ATOM 2326 CD PRO B 421 35.430 20.002 143.846 1.00 31.47 B C ATOM 2327 CA PRO B 421 37.177 18.376 143.455 1.00 31.76 B C ATOM 2328 CB PRO B 421 36.033 17.783 144.277 1.00 32.37 B C ATOM 2329 CG PRO B 421 34.869 18.597 143.833 1.00 31.84 B C ATOM 2330 C PRO B 421 37.462 17.536 142.212 1.00 32.82 B C ATOM 2331 O PRO B 421 37.890 16.383 142.329 1.00 33.44 B O ATOM 2332 N MET B 422 37.225 18.078 141.028 1.00 34.03 B N ATOM 2333 CA MET B 422 37.469 17.303 139.819 1.00 34.21 B C ATOM 2334 CB MET B 422 36.156 17.127 139.050 1.00 40.49 B C ATOM 2335 CG MET B 422 35.093 16.379 139.863 1.00 46.52 B C ATOM 2336 SD MET B 422 33.548 16.039 138.978 1.00 54.83 B S ATOM 2337 CE MET B 422 33.899 14.421 138.287 1.00 48.46 B C ATOM 2338 C MET B 422 38.520 17.987 138.965 1.00 30.07 B C ATOM 2339 O MET B 422 38.610 19.208 138.960 1.00 27.30 B O ATOM 2340 N TYR B 423 39.328 17.205 138.256 1.00 30.57 B N ATOM 2341 CA TYR B 423 40.386 17.789 137.423 1.00 30.47 B C ATOM 2342 CB TYR B 423 41.432 16.730 137.066 1.00 28.25 B C ATOM 2343 CG TYR B 423 42.541 17.261 136.179 1.00 28.83 B C ATOM 2344 CD1 TYR B 423 43.549 18.077 136.695 1.00 26.05 B C ATOM 2345 CE1 TYR B 423 44.547 18.607 135.866 1.00 26.97 B C ATOM 2346 CD2 TYR B 423 42.557 16.984 134.809 1.00 29.17 B C ATOM 2347 CE2 TYR B 423 43.548 17.509 133.973 1.00 28.79 B C ATOM 2348 GZ TYR B 423 44.537 18.319 134.508 1.00 27.46 B C ATOM 2349 OH TYR B 423 45.499 18.848 133.679 1.00 29.00 B O ATOM 2350 C TYR B 423 39.891 18.450 136.132 1.00 29.81 B C ATOM 2351 O TYR B 423 38.997 17.941 135.456 1.00 28.16 B O ATOM 2352 N ALA B 424 40.496 19.583 135.795 1.00 30.84 B N ATOM 2353 CA ALA B 424 40.155 20.320 134.582 1.00 30.74 B C ATOM 2354 CB ALA B 424 38.891 21.137 134.809 1.00 30.80 B C ATOM 2355 C ALA B 424 41.316 21.241 134.201 1.00 31.98 B C ATOM 2356 O ALA B 424 41.662 22.147 134.960 1.00 30.87 B O ATOM 2357 N PHE B 425 41.916 21.016 133.030 1.00 32.65 B N ATOM 2358 CA PHE B 425 43.037 21.847 132.587 1.00 32.21 B C ATOM 2359 CB PHE B 425 43.761 21.219 131.387 1.00 29.42 B C ATOM 2360 CG PHE B 425 44.871 22.085 130.837 1.00 28.07 B C ATOM 2361 CD1 PHE B 425 44.635 22.967 129.783 1.00 26.46 B C ATOM 2362 CD2 PHE B 425 46.130 22.075 131.427 1.00 26.10 B C ATOM 2363 GE1 PHE B 425 45.636 23.828 129.334 1.00 26.71 B C ATOM 2364 CE2 PHE B 425 47.138 22.933 130.986 1.00 23.65 B C ATOM 2365 CZ PHE B 425 46.890 23.811 129.941 1.00 24.65 B C ATOM 2366 C PHE B 425 42.612 23.261 132.226 1.00 32.08 B C ATOM 2367 O PHE B 425 41.517 23.474 131.723 1.00 35.15 B O ATOM 2368 N THR B 426 43.489 24.226 132.480 1.00 32.53 B N ATOM 2369 CA THR B 426 43.193 25.618 132.170 1.00 31.99 B C ATOM 2370 CB THR B 426 42.377 26.297 133.309 1.00 33.76 B C ATOM 2371 OG1 THR B 426 42.153 27.674 132.979 1.00 35.23 B O ATOM 2372 OG2 TER B 426 43.132 26.236 134.638 1.00 32.87 B C ATOM 2373 C THR B 426 44.470 26.415 131.960 1.00 32.40 B C ATOM 2374 O THR B 426 45.515 26.082 132.515 1.00 31.41 B O ATOM 2375 N GLU B 427 44.376 27.458 131.143 1.00 32.69 B N ATOM 2376 CA GLU B 427 45.505 28.338 130.877 1.00 34.12 B C ATOM 2377 CB GLU B 427 45.593 28.670 129.384 1.00 36.51 B C ATOM 2378 CG GLU B 427 45.967 27.493 128.490 1.00 41.69 B C ATOM 2379 CD GLU B 427 46.103 27.888 127.024 1.00 45.50 B C ATOM 2380 OE1 GLU B 427 45.082 28.269 126.410 1.00 44.55 B O ATOM 2381 OE2 GLU B 427 47.235 27.822 126.488 1.00 47.29 B O ATOM 2382 C GLU B 427 45.237 29.605 131.680 1.00 33.67 B C ATOM 2383 O GLU B 427 44.133 29.793 132.186 1.00 35.20 B O ATOM 2384 N GLY B 428 46.234 30.471 131.800 1.00 33.34 B N ATOM 2385 CA GLY B 428 46.041 31.692 132.561 1.00 34.51 B C ATOM 2386 C GLY B 428 46.066 31.428 134.057 1.00 36.70 B C ATOM 2387 O GLY B 428 46.241 30.281 134.475 1.00 35.95 B O ATOM 2388 N PRO B 429 45.887 32.468 134.893 1.00 37.61 B N ATOM 2389 CD PRO B 429 45.427 33.803 134.473 1.00 37.68 B C ATOM 2390 CA PRO B 429 45.888 32.363 136.361 1.00 35.27 B C ATOM 2391 CB PRO B 429 45.444 33.753 136.806 1.00 36.80 B C ATOM 2392 CG PRO B 429 44.594 34.224 135.655 1.00 38.82 B C ATOM 2393 C PRO B 429 44.969 31.258 136.882 1.00 34.51 B C ATOM 2394 O PRO B 429 43.769 31.248 136.605 1.00 35.20 B O ATOM 2395 N PRO B 430 45.533 30.312 137.648 1.00 32.84 B N ATOM 2396 CD PRO B 430 46.984 30.207 137.866 1.00 30.88 B C ATOM 2397 CA PRO B 430 44.843 29.160 138.246 1.00 33.23 B C ATOM 2398 CB PRO B 430 45.997 28.284 138.747 1.00 32.15 B C ATOM 2399 CG PRO B 430 47.172 28.722 137.930 1.00 32.06 B C ATOM 2400 C PRO B 430 43.870 29.482 139.381 1.00 33.86 B C ATOM 2401 O PRO B 430 42.786 28.891 139.475 1.00 32.09 B O ATOM 2402 N LEU B 431 44.271 30.405 140.250 1.00 34.56 B N ATOM 2403 CA LEU B 431 43.456 30.778 141.401 1.00 35.70 B C ATOM 2404 CB LEU B 431 44.300 31.550 142.419 1.00 33.79 B C ATOM 2405 CG LEU B 431 45.449 30.793 143.080 1.00 33.47 B C ATOM 2406 CD1 LEU B 431 46.049 31.651 144.190 1.00 33.46 B C ATOM 2407 CD2 LEU B 431 44.934 29.481 143.649 1.00 36.47 B C ATOM 2408 C LEU B 431 42.207 31.588 141.084 1.00 36.24 B C ATOM 2409 O LEU B 431 42.271 32.661 140.479 1.00 36.37 B O ATOM 2410 N HIS B 432 41.064 31.064 141.505 1.00 36.71 B N ATOM 2411 CA HIS B 432 39.811 31.760 141.299 1.00 41.25 B C ATOM 2412 CB HIS B 432 38.662 30.761 141.191 1.00 40.99 B C ATOM 2413 CG HIS B 432 37.332 31.404 140.963 1.00 44.68 B C ATOM 2414 CD2 HIS B 432 36.589 31.541 139.838 1.00 44.42 B C ATOM 2415 ND1 HIS B 432 36.626 32.031 141.967 1.00 46.47 B N ATOM 2416 CE1 HIS B 432 35.504 32.524 141.472 1.00 45.59 B C ATOM 2417 NB2 HIS B 432 35.459 32.241 140.182 1.00 46.62 B N ATOM 2418 C HIS B 432 39.613 32.670 142.507 1.00 44.37 B C ATOM 2419 O HIS B 432 40.151 32.400 143.588 1.00 46.02 B 0 ATOM 2420 N LYS B 433 38.859 33.751 142.330 1.00 46.58 B N ATOM 2421 CA LYS B 433 38.627 34.678 143.428 1.00 46.70 B C ATOM 2422 CB LYS B 433 37.717 35.822 142.972 1.00 51.43 B C ATOM 2423 CG LYS B 433 38.355 36.668 141.865 1.00 55.90 B C ATOM 2424 CD LYS B 433 37.589 37.956 141.584 1.00 59.77 B C ATOM 2425 CE LYS B 433 38.320 38.811 140.549 1.00 61.80 B C ATOM 2426 NZ LYS B 433 37.720 40.171 140.380 1.00 62.64 B N ATOM 2427 C LYS B 433 38.062 33.973 144.658 1.00 43.89 B C ATOM 2428 O LYS B 433 38.150 34.491 145.767 1.00 44.99 B O ATOM 2429 N ASP B 434 37.501 32.783 144.460 1.00 40.87 B N ATOM 2430 CA ASP B 434 36.964 31.998 145.565 1.00 39.24 B C ATOM 2431 CB ASP B 434 36.032 30.905 145.038 1.00 38.77 B C ATOM 2432 CG ASP B 434 35.520 29.999 146.138 1.00 39.93 B C ATOM 2433 OD1 ASP B 434 36.053 28.882 146.286 1.00 43.55 B O ATOM 2434 OD2 ASP B 434 34.593 30.408 146.866 1.00 42.42 B O ATOM 2435 C ASP B 434 38.127 31.365 146.337 1.00 40.97 B C ATOM 2436 O ASP B 434 38.102 31.288 147.571 1.00 41.38 B O ATOM 2437 N ASP B 435 39.144 30.915 145.601 1.00 39.44 B N ATOM 2438 CA ASP B 435 40.324 30.305 146.204 1.00 37.18 B C ATOM 2439 CB ASP B 435 41.258 29.737 145.128 1.00 36.04 B C ATOM 2440 CG ASP B 435 40.608 28.653 144.293 1.00 37.10 B C ATOM 2441 OD1 ASP B 435 40.086 27.671 144.868 1.00 35.74 B O ATOM 2442 OD2 ASP B 435 40.632 28.779 143.050 1.00 40.79 B O ATOM 2443 C ASP B 435 41.088 31.354 147.007 1.00 38.01 B C ATOM 2444 O ASP B 435 41.591 31.077 148.098 1.00 39.15 B O ATOM 2445 N VAL B 436 41.178 32.560 146.459 1.00 37.34 B N ATOM 2446 CA VAL B 436 41.893 33.637 147.127 1.00 37.88 B C ATOM 2447 CB VAL B 436 42.018 34.863 146.209 1.00 37.00 B C ATOM 2448 CG1 VAL B 436 42.850 35.939 146.887 1.00 37.16 B C ATOM 2449 CO2 VAL B 436 42.654 34.454 144.893 1.00 37.45 B C ATOM 2450 C VAL B 436 41.203 34.051 148.426 1.00 41.35 B C ATOM 2451 O VAL B 436 41.870 34.444 149.392 1.00 40.58 B O ATOM 2452 N ASN B 437 39.872 33.964 148.445 1.00 42.61 B N ATOM 2453 CA ASN B 437 39.103 34.323 149.633 1.00 42.98 B C ATOM 2454 CB ASN B 437 37.602 34.372 149.331 1.00 44.38 B C ATOM 2455 CG ASN B 437 37.199 35.607 148.564 1.00 46.07 B C ATOM 2456 OD1 ASN B 437 37.778 36.681 148.743 1.00 49.54 B O ATOM 2457 ND2 ASN B 437 36.182 35.471 147.721 1.00 46.44 B N ATOM 2458 C ASN B 437 39.341 33.309 150.732 1.00 41.97 B C ATOM 2459 O ASN B 437 39.656 33.665 151.863 1.00 44.18 B O ATOM 2460 N GLY B 438 39.177 32.038 150.391 1.00 42.23 B N ATOM 2461 CA GLY B 438 39.373 30.980 151.364 1.00 41.20 B C ATOM 2462 C GLY B 438 40.737 31.015 152.030 1.00 40.27 B C ATOM 2463 O GLY B 438 40.851 30.821 153.241 1.00 40.43 B O ATOM 2464 N 1LE B 439 41.778 31.269 151.246 1.00 39.21 B N ATOM 2465 CA ILE B 439 43.125 31.305 151.796 1.00 38.89 B C ATOM 2466 CB 1LE B 439 44.195 31.186 150.666 1.00 34.85 B C ATOM 2467 CG2 RE B 439 44.318 32.488 149.913 1.00 32.27 B C ATOM 2468 CG1 ILE B 439 45.546 30.783 151.262 1.00 34.00 B C ATOM 2469 CD1 ILE B 439 45.558 29.373 151.853 1.00 32.09 B C ATOM 2470 C ILE B 439 43.317 32.597 152.587 1.00 40.47 B C ATOM 2471 O ILE B 439 44.034 32.625 153.588 1.00 41.20 B O ATOM 2472 N ARG B 440 42.654 33.658 152.134 1.00 43.75 B N ATOM 2473 CA ARG B 440 42.725 34.967 152.782 1.00 44.46 B C ATOM 2474 CB ARG B 440 42.048 36.030 151.909 1.00 46.94 B C ATOM 2475 CG ARG B 440 42.937 37.185 151.471 1.00 49.56 B C ATOM 2476 CD ARG B 440 43.845 36.769 150.334 1.00 54.73 B C ATOM 2477 NE ARG B 440 44.726 37.850 149.901 1.00 58.03 B N ATOM 2478 CZ ARG B 440 44.306 38.991 149.362 1.00 60.42 B C ATOM 2479 NH1 ARG B 440 43.009 39.211 149.186 1.00 60.93 B N ATOM 2480 NH2 ARG B 440 45.188 39.910 148.988 1.00 60.50 B N ATOM 2481 C ARG B 440 42.006 34.908 154.128 1.00 44.17 B C ATOM 2482 O ARG B 440 42.320 35.666 155.047 1.00 43.24 B O ATOM 2483 N HIS B 441 41.033 34.004 154.221 1.00 42.88 B N ATOM 2484 CA HIS B 441 40.235 33.818 155.428 1.00 43.46 B C ATOM 2485 CB HIS B 441 38.997 32.972 155.112 1.00 46.73 B C ATOM 2486 CG HIS B 441 38.118 32.713 156.297 1.00 52.22 B C ATOM 2487 CD2 HIS B 441 37.906 31.588 157.022 1.00 53.91 B C ATOM 2488 ND1 HIS B 441 37.331 33.690 156.871 1.00 54.78 B N ATOM 2489 CE1 HIS B 441 36.673 33.178 157.896 1.00 54.20 B C ATOM 2490 NR2 HIS B 441 37.005 31.904 158.010 1.00 54.76 B N ATOM 2491 C HIS B 441 41.029 33.144 156.538 1.00 42.38 B C ATOM 2492 O HIS B 441 40.835 33.448 157.713 1.00 43.43 B O ATOM 2493 N LEU B 442 41.924 32.233 156.158 1.00 40.54 B N ATOM 2494 CA LEU B 442 42.747 31.495 157.118 1.00 37.84 B C ATOM 2495 GB LEU B 442 43.136 30.124 156.542 1.00 36.23 B C ATOM 2496 CG LEU B 442 42.020 29.121 156.224 1.00 36.95 B C ATOM 2497 CD1 LEU B 442 42.600 27.921 155.494 1.00 37.45 B C ATOM 2498 CD2 LEU B 442 41.337 28.676 157.507 1.00 38.67 B C ATOM 2499 C LEU B 442 44.012 32.232 157.548 1.00 35.29 B C ATOM 2500 O LEU B 442 44.367 32.218 158.721 1.00 37.44 B O ATOM 2501 N TYR B 443 44.693 32.872 156.605 1.00 34.38 B N ATOM 2502 CA TYR B 443 45.932 33.581 156.920 1.00 36.23 B C ATOM 2503 GB TYR B 443 47.105 32.984 156.123 1.00 34.25 B C ATOM 2504 CG TYR B 443 47.261 31.490 156.300 1.00 31.93 B C ATOM 2505 CD1 TYR B 443 46.614 30.596 155.446 1.00 29.81 B C ATOM 2506 CE1 TYR B 443 46.695 29.215 155.649 1.00 28.03 B C ATOM 2507 CD2 TYR B 443 48.004 30.968 157.366 1.00 29.17 B C ATOM 2508 CE2 TYR B 443 48.092 29.592 157.578 1.00 28.10 B C ATOM 2509 CZ TYR B 443 47.433 28.721 156.718 1.00 29.15 B C ATOM 2510 OH TYR B 443 47.496 27.360 156.932 1.00 27.85 B O ATOM 2511 C TYR B 443 45.855 35.082 156.659 1.00 38.24 B C ATOM 2512 O TYR B 443 46.801 35.794 157.063 1.00 40.58 B O ATOM 2513 OT TYR B 443 44.864 35.527 156.044 1.00 41.15 B O ATOM 2562 ZN ZN B 1 41.275 17.840 146.537 1.00 30.01 Z ZN ATOM 2563 ZN ZN B 2 49.676 8.887 150.296 1.00 22.73 Z ZN ATOM 2570 CA CA B 3 54.013 17.086 157.486 1.00 25.83 C C ATOM 2571 CA CA B 4 54.046 8.303 135.827 1.00 47.76 C C ATOM 2572 CA CA B 5 50.701 18.541 128.694 1.00 57.49 C C ATOM 2569 CA CA B 6 45.250 7.241 139.948 1.00 21.01 C C ATOM 2574 CA CA B 7 53.492 38.165 150.097 1.00 99.62 C C ATOM 2537 C1 FRA B 2 40.988 17.843 141.282 1.00 21.42 M C ATOM 2538 C2 FRA B 2 42.202 16.892 141.164 1.00 23.04 M C ATOM 2539 C3 FRA B 2 43.397 17.813 140.945 1.00 21.68 M C ATOM 2540 C4 FRA B 2 42.395 16.088 142.486 1.00 20.53 M C ATOM 2541 C5 FRA B 2 41.287 15.047 142.944 1.00 22.68 M C ATOM 2542 C6 FRA B 2 41.674 14.384 144.328 1.00 21.04 M C ATOM 2543 N7 FRA B 2 41.894 15.346 145.441 1.00 26.66 M N ATOM 2544 C8 FRA B 2 40.878 16.003 145.917 1.00 16.04 M O ATOM 2545 C9 FRA B 2 43.101 15.578 145.982 1.00 25.43 M C ATOM 2546 C10 FRA B 2 43.304 16.343 146.865 1.00 27.78 M O ATOM 2547 C11 FRA B 2 41.103 13.852 141.935 1.00 24.21 M C ATOM 2548 N12 FRA B 2 39.910 13.731 141.312 1.00 24.87 M N ATOM 2549 C13 FRA B 2 39.558 12.636 140.307 1.00 25.69 M C ATOM 2550 C14 FRA B 2 38.064 12.068 140.550 1.00 26.41 M C ATOM 25S1 C15 FRA B 2 37.671 10.934 139.534 1.00 23.S4 M C ATOM 2S52 C16 FRA B 2 36.936 13.161 140.404 1.00 25.14 M C ATOM 2553 C17 FRA B 2 37.918 11.501 141.991 1.00 25.52 M C ATOM 2554 C18 FRA B 2 39.789 13.241 138.843 1.00 26.03 M C ATOM 2555 O19 FRA B 2 39.414 14.401 138.550 1.00 27.42 M O ATOM 2556 N20 FRA B 2 40.416 12.393 137.981 1.00 25.15 M N ATOM 2557 C21 FRA B 2 40.752 12.702 136.573 1.00 30.05 M C ATOM 2558 022 FRA B 2 42.049 13.051 141.732 1.00 25.04 M O ATOM 2576 O HOE W 1 53.372 24.644 125.318 1.00 1.00 W O ATOM 2577 O HON W 2 74.083 20.414 120.913 1.00 21.76 W O ATOM 2578 O HOH W 3 49.364 12.911 104.335 1.00 26.01 W O ATOM 2579 O HON W 4 52.1M 16.494 124.475 1.00 14.30 W O ATOM 2580 O HOH W 5 58.587 7.014 115.292 1.00 27.11 W O ATOM 2581 O HOH W 6 75.605 18.864 112.249 1.00 18.56 W O ATOM 2582 O HOH W 7 65.295 7.257 120.405 1.00 1.00 W O ATOM 2583 O HOH W 8 57.185 8.107 113.191 1.00 17.03 W O ATOM 2584 O HOH W 9 64.469 12.077 98.818 1.00 47.82 W O ATOM 2585 O HOH W 10 51.666 21.908 124.829 1.00 15.33 W O ATOM 2586 O HOH W 11 67.629 24.639 127.665 1.00 20.55 W O ATOM 2587 O HOH W 12 67.365 14.751 108.625 1.00 21.02 W O ATOM 2588 O HOH W 13 52.957 12.041 116.137 1.00 15.20 W O ATOM 2589 O HOH W 14 51.253 9.646 116.663 1.00 29.59 W O ATOM 2590 O HOH W 15 48.380 16.148 113.137 1.00 26.43 W O ATOM 2591 O HOH W 16 49.177 9.855 111.408 1.00 25.21 W O ATOM 2592 O HOH W 17 56.870 18.582 90.415 1.00 50.62 W O ATOM 2593 O HON W 18 56.995 17.921 96.140 1.00 26.85 W O ATOM 2594 O HOH W 19 61.756 9.877 125.515 1.00 40.50 W O ATOM 2595 O HON W 20 45.873 28.448 97.477 1.00 25.98 W O ATOM 2596 O HOH W 21 50.275 10.441 122.477 1.00 33.64 W O ATOM 2597 O HON W 22 56.828 39.659 107.746 1.00 37.53 W O ATOM 2598 O HOH W 23 56.922 8.730 101.984 1.00 51.25 W O ATOM 2599 O HOH W 24 63.090 12.420 103.873 1.00 23.17 W O ATOM 2600 O HOH W 25 78.432 18.341 111.530 1.00 33.10 W O ATOM 2601 O HOH W 26 55.278 7.063 126.543 1.00 22.51 W O ATOM 2602 O HOH W 27 71.699 14.944 110.281 1.00 31.13 W O ATOM 2603 O HON W 28 65.856 12.461 105.207 1.00 34.23 W O ATOM 2604 O HOH W 29 49.226 13.404 112.556 1.00 36.10 W O ATOM 2605 O HON W 30 45.806 26.797 113.582 1.00 25.06 W O ATOM 2606 O HOH W 31 50.921 22.489 96.419 1.00 38.17 W O ATOM 2607 O HOH W 32 47.043 17.179 110.619 1.00 27.88 W O ATOM 2608 O HOH W 33 50.505 31.197 136.475 1.00 33.10 W O ATOM 2609 O HOH W 34 47.341 22.271 121.211 1.00 20.31 W O ATOM 2610 O HOH W 35 61.912 15.434 101.221 1.00 22.75 W O ATOM 2611 O HOH W 36 70.118 14.389 108.156 1.00 55.54 W O ATOM 2612 O HOH W 37 60.170 4.215 113.980 1.00 40.21 W O ATOM 2613 O HOH W 38 50.540 23.541 133.215 1.00 2.46 W O ATOM 2614 O HOH W 39 48.871 4.037 141.580 1.00 13.61 W O ATOM 2615 O HOH W 40 59.625 29.594 154.497 1.00 17.76 W O ATOM 2616 O HOH W 41 58.300 23.513 135.522 1.00 22.04 W O ATOM 2617 O HOH W 42 64.850 17.232 147.313 1.00 21.84 W O ATOM 2618 O HOH W 43 49.326 3.982 150.548 1.00 24.48 W O ATOM 2619 O HOH W 45 63.774 19.112 148.870 1.00 12.98 W O ATOM 2620 O HON W 46 55.863 15.629 163.760 1.00 28.09 W O ATOM 2621 O HON W 47 53.389 24.883 133.848 1.00 20.87 W O ATOM 2622 O HOH W 48 47.215 9.463 133.451 1.00 38.63 W O ATOM 2623 O HOH W 49 54.340 11.753 153.786 1.00 25.99 W O ATOM 2624 O HOH W 50 61.472 23.563 144.309 1.00 18.90 W O ATOM 2625 O HOH W 51 63.912 24.339 144.017 1.00 19.40 W O ATOM 2626 O HOH W 52 58.245 29.246 145.388 1.00 26.64 W O ATOM 2627 O HOH W 53 63.745 27.746 148.959 1.00 20.88 W O ATOM 2628 O HOH W 54 51.102 26.318 167.875 1.00 28.44 W O ATOM 2629 O HON W 55 52.106 25.451 162.757 1.00 26.05 W O ATOM 2630 O HOH W 56 62.401 12.111 136.745 1.00 22.15 W O ATOM 2631 O HOH W 57 45.079 38.240 157.288 1.00 46.25 W O ATOM 2632 O HOH W 58 64.533 23.652 138.613 1.00 23.45 W O ATOM 2633 O HOH W 59 32.586 28.259 147.755 1.00 53.44 W O ATOM 2634 O HOH W 60 60.965 22.491 159.169 1.00 36.88 W O ATOM 2635 O HOH W 61 56.540 16.675 157.926 1.00 22.67 W O ATOM 2636 O HOH W 62 49.724 1.457 152.163 1.00 31.25 W O ATOM 2637 O HOH W 63 66.979 17.779 135.834 1.00 30.64 W O ATOM 2638 O HOH W 64 53.679 7.411 152.678 1.00 24.59 W O ATOM 2639 O HOH W 65 55.862 13.242 157.045 1.00 22.19 W O ATOM 2640 O HOH W 66 60.317 27.514 146.861 1.00 50.28 W O ATOM 2641 O HOH W 67 48.564 34.049 142.813 1.00 37.03 W O ATOM 2642 O HOH W 68 47.734 34.009 159.841 1.00 57.14 W O ATOM 2643 O HOH W 69 56.949 31.429 147.112 1.00 30.39 W O ATOM 2644 O HOH W 70 47.008 25.477 120.702 1.00 23.76 W O ATOM 2645 O HOH W 71 53.453 29.741 136.903 1.00 25.90 W O ATOM 2646 O HOH W 72 54.023 18.711 159.706 1.00 18.27 W O ATOM 2647 O HOH W 73 54.530 9.056 154.663 1.00 34.56 W O ATOM 2648 O HOH W 74 66.399 14.925 149.889 1.00 36.21 W O ATOM 2649 O HOH W 75 56.078 0.717 148.547 1.00 47.62 W O ATOM 2650 O HOH W 76 55.037 3.104 145.929 1.00 22.70 W O ATOM 2651 O HOH W 77 57.979 5.727 117.915 1.00 65.95 W O ATOM 2652 O HOH W 78 38.602 9.525 136.215 1.00 34.41 W O ATOM 2653 O HOH W 79 56.644 33.927 107.571 1.00 25.40 W O ATOM 2654 O HOH W 80 56.901 12.608 98.500 1.00 45.22 W O ATOM 2655 O HOH W 81 66.159 25.939 129.659 1.00 45.73 W O ATOM 2656 O HOH W 82 52.849 33.406 118.492 1.00 33.45 W O ATOM 2657 O HOH W 83 40.064 12.132 132.917 1.00 45.44 W O ATOM 2658 O HOH W 84 61.356 7.072 144.041 1.00 52.29 W O ATOM 2659 O HOH W 85 59.332 33.793 126.661 1.00 37.65 W O ATOM 2660 O HOH W 86 76.248 14.005 117.780 1.00 38.05 W O ATOM 2661 O HOH W 87 63.920 4.959 114.145 1.00 28.43 W O ATOM 2662 O HOH W 88 41.594 23.567 106.694 1.00 35.95 W O ATOM 2663 O HOH W 89 43.961 20.340 105.825 1.00 34.92 W O ATOM 2664 O HOH W 90 73.852 13.594 117.386 1.00 26.01 W O ATOM 2665 O HOH W 91 59.941 14.152 100.157 1.00 27.50 W O ATOM 2666 O HOH W 92 59.242 23.420 132.602 1.00 16.67 W O ATOM 2667 O HOH W 93 58.837 25.317 128.952 1.00 21.05 W O ATOM 2668 O HOH W 94 51.613 25.829 131.530 1.00 40.97 W O ATOM 2669 O HOH W 95 64.674 28.352 131.418 1.00 31.06 W O ATOM 2670 O HOH W 96 60.935 29.269 136.385 1.00 24.27 W O ATOM 2671 O HOH W 97 54.832 34.703 109.520 1.00 17.56 W O ATOM 2672 O HOH W 98 58.791 32.739 117.544 1.00 24.04 W O ATOM 2673 O HOH W 99 56.442 35.249 118.352 1.00 28.89 W O ATOM 2674 O HOH W 100 46.526 37.510 114.770 1.00 35.71 W O ATOM 2675 O HOH W 1O1 54.579 35.721 151.192 1.00 51.01 W O ATOM 2676 O HOH W 102 58.105 32.269 149.264 1.00 23.65 W O ATOM 2677 O HOH W 103 65.313 13.049 157.092 1.00 26.96 W O ATOM 2678 O HOH W 104 66.201 11.386 155.250 1.00 48.24 W O ATOM 2679 O HOH W 105 53.996 0.840 145.922 1.00 34.76 W O ATOM 2680 O HOH W 106 46.202 0.833 136.125 1.00 47.74 W O ATOM 2681 O HOH W 1O7 56.086 6.461 135.385 1.00 47.82 W O ATOM 2682 O HOH W 108 51.570 16.588 127.129 1.00 18.01 W O ATOM 2683 O HOH W 109 46.668 19.140 128.889 1.00 23.88 W O ATOM 2684 O HOH W 110 45.451 12.416 128.248 1.00 32.22 W O ATOM 2685 O HOH W 111 53.514 30.754 139.864 1.00 31.81 W O ATOM 2686 O HOH W 112 52.273 39.562 147.763 1.00 51.12 W O ATOM 2687 O HOH W 113 52.591 10.981 161.536 1.00 34.69 W O ATOM 2688 O HOH W 114 50.264 24.639 126.956 1.00 19.43 W O ATOM 2689 O HOH W 115 45.122 15.259 128.545 1.00 36.82 W O ATOM 2690 O HOH W 116 45.881 15.698 122.389 1.00 39.53 W O ATOM 2691 O HOH W 117 45.448 17.802 130.938 1.00 37.87 W O ATOM 2692 O HOH W 118 58.454 6.855 127.071 1.00 27.25 W O ATOM 2693 O HOH W 119 62.131 28.235 104.517 1.00 40.71 W O ATOM 2694 O HOH W 120 66.292 32.682 114.288 1.00 25.89 W O ATOM 2695 O HOH W 121 65.759 26.751 110.354 1.00 19.28 W O END

[0136]

1 2 1 660 PRT Homo sapiens 1 Met Glu Ala Leu Met Ala Arg Gly Ala Leu Thr Gly Pro Leu Arg Ala 1 5 10 15 Leu Cys Leu Leu Gly Cys Leu Leu Ser His Ala Ala Ala Ala Pro Ser 20 25 30 Pro Ile Ile Lys Phe Pro Gly Asp Val Ala Pro Lys Thr Asp Lys Glu 35 40 45 Leu Ala Val Gln Tyr Leu Asn Thr Phe Tyr Gly Cys Pro Lys Glu Ser 50 55 60 Cys Asn Leu Phe Val Leu Lys Asp Thr Leu Lys Lys Met Gln Lys Phe 65 70 75 80 Phe Gly Leu Pro Gln Thr Gly Asp Leu Asp Gln Asn Thr Ile Glu Thr 85 90 95 Met Arg Lys Pro Arg Cys Gly Asn Pro Asp Val Ala Asn Tyr Asn Phe 100 105 110 Phe Pro Arg Lys Pro Lys Trp Asp Lys Asn Gln Ile Thr Tyr Arg Ile 115 120 125 Ile Gly Tyr Thr Pro Asp Leu Asp Pro Glu Thr Val Asp Asp Ala Phe 130 135 140 Ala Arg Ala Phe Gln Val Trp Ser Asp Val Thr Pro Leu Arg Phe Ser 145 150 155 160 Arg Ile His Asp Gly Glu Ala Asp Ile Met Ile Asn Phe Gly Arg Trp 165 170 175 Glu His Gly Asp Gly Tyr Pro Phe Asp Gly Lys Asp Gly Leu Leu Ala 180 185 190 His Ala Phe Ala Pro Gly Thr Gly Val Gly Gly Asp Ser His Phe Asp 195 200 205 Asp Asp Glu Leu Trp Thr Leu Gly Glu Gly Gln Val Val Arg Val Lys 210 215 220 Tyr Gly Asn Ala Asp Gly Glu Tyr Cys Lys Phe Pro Phe Leu Phe Asn 225 230 235 240 Gly Lys Glu Tyr Asn Ser Cys Thr Asp Thr Gly Arg Ser Asp Gly Phe 245 250 255 Leu Trp Cys Ser Thr Thr Tyr Asn Phe Glu Lys Asp Gly Lys Tyr Gly 260 265 270 Phe Cys Pro His Glu Ala Leu Phe Thr Met Gly Gly Asn Ala Glu Gly 275 280 285 Gln Pro Cys Lys Phe Pro Phe Arg Phe Gln Gly Thr Ser Tyr Asp Ser 290 295 300 Cys Thr Thr Glu Gly Arg Thr Asp Gly Tyr Arg Trp Cys Gly Thr Thr 305 310 315 320 Glu Asp Tyr Asp Arg Asp Lys Lys Tyr Gly Phe Cys Pro Glu Thr Ala 325 330 335 Met Ser Thr Val Gly Gly Asn Ser Glu Gly Ala Pro Cys Val Phe Pro 340 345 350 Phe Thr Phe Leu Gly Asn Lys Tyr Glu Ser Cys Thr Ser Ala Gly Arg 355 360 365 Ser Asp Gly Lys Met Trp Cys Ala Thr Thr Ala Asn Tyr Asp Asp Asp 370 375 380 Arg Lys Trp Gly Phe Cys Pro Asp Gln Gly Tyr Ser Leu Phe Leu Val 385 390 395 400 Ala Ala His Glu Phe Gly His Ala Met Gly Leu Glu His Ser Gln Asp 405 410 415 Pro Gly Ala Leu Met Ala Pro Ile Tyr Thr Tyr Thr Lys Asn Phe Arg 420 425 430 Leu Ser Gln Asp Asp Ile Lys Gly Ile Gln Glu Leu Tyr Gly Ala Ser 435 440 445 Pro Asp Ile Asp Leu Gly Thr Gly Pro Thr Pro Thr Leu Gly Pro Val 450 455 460 Thr Pro Glu Ile Cys Lys Gln Asp Ile Val Phe Asp Gly Ile Ala Gln 465 470 475 480 Ile Arg Gly Glu Ile Phe Phe Phe Lys Asp Arg Phe Ile Trp Arg Thr 485 490 495 Val Thr Pro Arg Asp Lys Pro Met Gly Pro Leu Leu Val Ala Thr Phe 500 505 510 Trp Pro Glu Leu Pro Glu Lys Ile Asp Ala Val Tyr Glu Ala Pro Gln 515 520 525 Glu Glu Lys Ala Val Phe Phe Ala Gly Asn Glu Tyr Trp Ile Tyr Ser 530 535 540 Ala Ser Thr Leu Glu Arg Gly Tyr Pro Lys Pro Leu Thr Ser Leu Gly 545 550 555 560 Leu Pro Pro Asp Val Gln Arg Val Asp Ala Ala Phe Asn Trp Ser Lys 565 570 575 Asn Lys Lys Thr Tyr Ile Phe Ala Gly Asp Lys Phe Trp Arg Tyr Asn 580 585 590 Glu Val Lys Lys Lys Met Asp Pro Gly Phe Pro Lys Leu Ile Ala Asp 595 600 605 Ala Trp Asn Ala Ile Pro Asp Asn Leu Asp Ala Val Val Asp Leu Gln 610 615 620 Gly Gly Gly His Ser Tyr Phe Phe Lys Gly Ala Tyr Tyr Leu Lys Leu 625 630 635 640 Glu Asn Gln Ser Leu Lys Ser Val Lys Phe Gly Ser Ile Lys Ser Asp 645 650 655 Trp Leu Gly Cys 660 2 707 PRT Homo sapiens 2 Met Ser Leu Trp Gln Pro Leu Val Leu Val Leu Leu Val Leu Gly Cys 1 5 10 15 Cys Phe Ala Ala Pro Arg Gln Arg Gln Ser Thr Leu Val Leu Phe Pro 20 25 30 Gly Asp Leu Arg Thr Asn Leu Thr Asp Arg Gln Leu Ala Glu Glu Tyr 35 40 45 Leu Tyr Arg Tyr Gly Tyr Thr Arg Val Ala Glu Met Arg Gly Glu Ser 50 55 60 Lys Ser Leu Gly Pro Ala Leu Leu Leu Leu Gln Lys Gln Leu Ser Leu 65 70 75 80 Pro Glu Thr Gly Glu Leu Asp Ser Ala Thr Leu Lys Ala Met Arg Thr 85 90 95 Pro Arg Cys Gly Val Pro Asp Leu Gly Arg Phe Gln Thr Phe Glu Gly 100 105 110 Asp Leu Lys Trp His His His Asn Ile Thr Tyr Trp Ile Gln Asn Tyr 115 120 125 Ser Glu Asp Leu Pro Arg Ala Val Ile Asp Asp Ala Phe Ala Arg Ala 130 135 140 Phe Ala Leu Trp Ser Ala Val Thr Pro Leu Thr Phe Thr Arg Val Tyr 145 150 155 160 Ser Arg Asp Ala Asp Ile Val Ile Gln Phe Gly Val Ala Glu His Gly 165 170 175 Asp Gly Tyr Pro Phe Asp Gly Lys Asp Gly Leu Leu Ala His Ala Phe 180 185 190 Pro Pro Gly Pro Gly Ile Gln Gly Asp Ala His Phe Asp Asp Asp Glu 195 200 205 Leu Trp Ser Leu Gly Lys Gly Val Val Val Pro Thr Arg Phe Gly Asn 210 215 220 Ala Asp Gly Ala Ala Cys His Phe Pro Phe Ile Phe Glu Gly Arg Ser 225 230 235 240 Tyr Ser Ala Cys Thr Thr Asp Gly Arg Ser Asp Gly Leu Pro Trp Cys 245 250 255 Ser Thr Thr Ala Asn Tyr Asp Thr Asp Asp Arg Phe Gly Phe Cys Pro 260 265 270 Ser Glu Arg Leu Tyr Thr Arg Asp Gly Asn Ala Asp Gly Lys Pro Cys 275 280 285 Gln Phe Pro Phe Ile Phe Gln Gly Gln Ser Tyr Ser Ala Cys Thr Thr 290 295 300 Asp Gly Arg Ser Asp Gly Tyr Arg Trp Cys Ala Thr Thr Ala Asn Tyr 305 310 315 320 Asp Arg Asp Lys Leu Phe Gly Phe Cys Pro Thr Arg Ala Asp Ser Thr 325 330 335 Val Met Gly Gly Asn Ser Ala Gly Glu Leu Cys Val Phe Pro Phe Thr 340 345 350 Phe Leu Gly Lys Glu Tyr Ser Thr Cys Thr Ser Glu Gly Arg Gly Asp 355 360 365 Gly Arg Leu Trp Cys Ala Thr Thr Ser Asn Phe Asp Ser Asp Lys Lys 370 375 380 Trp Gly Phe Cys Pro Asp Gln Gly Tyr Ser Leu Phe Leu Val Ala Ala 385 390 395 400 His Glu Phe Gly His Ala Leu Gly Leu Asp His Ser Ser Val Pro Glu 405 410 415 Ala Leu Met Tyr Pro Met Tyr Arg Phe Thr Glu Gly Pro Pro Leu His 420 425 430 Lys Asp Asp Val Asn Gly Ile Arg His Leu Tyr Gly Pro Arg Pro Glu 435 440 445 Pro Glu Pro Arg Pro Pro Thr Thr Thr Thr Pro Gln Pro Thr Ala Pro 450 455 460 Pro Thr Val Cys Pro Thr Gly Pro Pro Thr Val His Pro Ser Glu Arg 465 470 475 480 Pro Thr Ala Gly Pro Thr Gly Pro Pro Ser Ala Gly Pro Thr Gly Pro 485 490 495 Pro Thr Ala Gly Pro Ser Thr Ala Thr Thr Val Pro Leu Ser Pro Val 500 505 510 Asp Asp Ala Cys Asn Val Asn Ile Phe Asp Ala Ile Ala Glu Ile Gly 515 520 525 Asn Gln Leu Tyr Leu Phe Lys Asp Gly Lys Tyr Trp Arg Phe Ser Glu 530 535 540 Gly Arg Gly Ser Arg Pro Gln Gly Pro Phe Leu Ile Ala Asp Lys Trp 545 550 555 560 Pro Ala Leu Pro Arg Lys Leu Asp Ser Val Phe Glu Glu Pro Leu Ser 565 570 575 Lys Lys Leu Phe Phe Phe Ser Gly Arg Gln Val Trp Val Tyr Thr Gly 580 585 590 Ala Ser Val Leu Gly Pro Arg Arg Leu Asp Lys Leu Gly Leu Gly Ala 595 600 605 Asp Val Ala Gln Val Thr Gly Ala Leu Arg Ser Gly Arg Gly Lys Met 610 615 620 Leu Leu Phe Ser Gly Arg Arg Leu Trp Arg Phe Asp Val Lys Ala Gln 625 630 635 640 Met Val Asp Pro Arg Ser Ala Ser Glu Val Asp Arg Met Phe Pro Gly 645 650 655 Val Pro Leu Asp Thr His Asp Val Phe Gln Tyr Arg Glu Lys Ala Tyr 660 665 670 Phe Cys Gln Asp Arg Phe Tyr Trp Arg Val Ser Ser Arg Ser Glu Leu 675 680 685 Asn Gln Val Asp Gln Val Gly Tyr Val Thr Tyr Asp Ile Leu Gln Cys 690 695 700 Pro Glu Asp 705 

What we claim is:
 1. A crystalline form of a polypeptide corresponding to the catalytic domain of an MMP9 protein.
 2. A crystalline form of a polypeptide corresponding to the catalytic domain of an MMP9 protein in complex with an MMP9 inhibitor compound.
 3. A crystalline form of a polypeptide corresponding to the active site binding region of an MMP9 protein wherein the active site binding region amino acid residues are identical or equivalent to those listed in Table 1 and the shape of the active site binding region is defined by the atomic coordinates given in Table 2 or Table 3 or by equivalent coordinates.
 4. A method to determine or design the three dimensional structure of a crystal form of MMP9 by difference Fourier or molecular replacement, using the atomic coordinates of a first MMP9 crystal to model the structure of a second MMP9 crystal wherein the active site binding region amino acid residues of the first MMP9 crystal are identical or equivalent to those listed in Table 1 and the shape of the active site binding region of the first MMP9 crystal is defined by the atomic coordinates given in Table 2 or Table 3 or by equivalent coordinates.
 5. An MMP9 protein designed by the method claimed in claim
 4. 6. A method to select or design a chemical modulator of MMP9 by selecting or designing a modulator with a three dimensional structure that fits into the MMP9 active site binding region, wherein the active site binding region amino acid residues are identical or equivalent to those listed in Table 1 and the shape of the active site binding region is defined by the atomic coordinates given in Table 2 or Table 3 or by equivalent coordinates.
 7. A modulator of MMP9 selected or designed by the method claimed in claim 6, or a pharmaceutically acceptable salt or in vivo hydrolysable ester thereof.
 8. Use of an MMP9 modulator selected or designed by the method claimed in claim 6, or a pharmaceutically acceptable salt or in vivo hydrolysable ester thereof, to treat a metalloproteinase mediated disease or condition.
 9. A method of treating a metalloproteinase mediated disease or condition which comprises administering to a warm-blooded animal a therapeutically effective amount of a modulator of MMP9 or a pharmaceutically acceptable salt or in vivo hydrolysable ester thereof, wherein the MMP9 modulator is selected or designed by the method claimed in claim
 6. 